The Academic Press FactsBook Series has established itself as the best source of easily-accessible and accurate facts about protein groups. Described as 'a growing series of excellent manuals' by Molecular Medicine Today and 'essential works of reference' by Trends in Biochemical Sciences, the FactsBooks have become the most popular comprehensive data resources available. Using an easy-to-follow format, the FactsBooks will keep you up-to-date with the latest advances in structure, amino acid sequences, physicochemical properties, and biological activity. Meticulously researched and compiled by experts in the field, keeping abreast of developments has never been so easy!
The Transporter FactsBook contains entries covering almost 800 transporters. Organized into 55 families of structurally related transporters, this volume includes ATPases, ABC transporters, H+-dependent antiporters and symporters, Na+-dependent antiporters and symporters, and other transporters such as mitochondrial transporters.
Key Features
* Nomenclature, biological sources and substrates
* Phylogenetic relationships
* Predicted structures
* Physical and genetic characteristics
* Multiple amino acid sequence alignments
* Database accession numbers
* Key references
How do you keep track of basic information on the proteins you work with? Where do you find details of their physicochemical properties, amino acid sequences, and structure? Are you tired of scanning review articles, primary papers, and databases to locate that elusive fact? The Academic Press FactsBook Series has established itself as the best source of easily-accessible and accurate facts about protein groups. Described as "e;a growing series of excellent manuals"e; by Molecular Medicine Today and "e;essential works of reference"e; by Trends in Biochemical Sciences, the FactsBooks have become the most popular comprehensive data resources available. Using an easy-to-follow format, the FactsBooks will keep you up-to-date with the latest advances in structure, amino acid sequences, physicochemical properties, and biological activity. Meticulously researched and compiled by experts in the field, keeping abreast of developments has never been so easy!The Transporter FactsBook contains entries covering almost 800 transporters. Organized into 55 families of structurally related transporters, this volume includes ATPases, ABC transporters, H+-dependent antiporters and symporters, Na+-dependent antiporters and symporters, and other transporters such as mitochondrial transporters. Nomenclature, biological sources and substrates Phylogenetic relationships Predicted structures Physical and genetic characteristics Multiple amino acid sequence alignments Database accession numbers Key references
Front Cover 1
The Transporter Facts Book 4
Copyright Page 5
Contents 6
Preface 10
Abbreviations 11
Section I: THE INTRODUCTORY CHAPTERS 12
Chapter 1. Function and Structure of Membrane Transport Proteins 14
Chapter 2. Amino Acid Sequence Comparisons 41
Chapter 3. Organization of the Data 45
Section II: THE MEMBRANE TRANSPORT PROTEINS 50
Part 1: P-Type ATPases 52
Chapter 4. Calcium-transporting ATPase family 53
Chapter 5. Plasma membrane cation-transporting ATPase family 59
Chapter 6. Heavy metal-transporting ATPase family 99
Part 2: Vacuolar ATPases 114
Chapter 7. Vacuolar ATPase family 115
Part 3: ABC Multidrug Resistance Proteins 124
Chapter 8. White transporter family 125
Chapter 9. ABC 1 & 2 transporter family
Chapter 10. Yeast multidrug resistance family 137
Chapter 11. Cystic fibrosis transmembrane conductance regulator family 146
Chapter 12. P-Glycoprotein transporter family 153
Chapter 13. Peroxisomal membrane transporter family 190
Part 4: ABCQ Transporters 196
Chapter 14. ABC-2 nodulation protein family 197
Chapter 15. ABC-2 polysaccharide exporter family 201
Chapter 16. ABC-2 associated (cytoplasmic) protein family 205
Part 5: ABC Binding Protein-Dependent Transporters: Transmembrane Elements 214
Chapter 17. ABC-associated binding protein-dependent maltose transporter family 215
Chapter 18. ABC-associated binding protein-dependent peptide transporter family 219
Chapter 19. ABC-associated binding protein-dependent iron transporter family 225
Part 6: ABC Binding Protein-Dependent Transporters: Cytoplasmic Elements 232
Chapter 20. Binding protein-dependent monosaccharide transporter family 233
Chapter 21. Binding protein-dependent peptide transporter family 238
Part 7: Other ABC-Associated (Cytoplasmic) Proteins 262
Chapter 22. Heme exporter family 263
Chapter 23. Macrolide-streptogramin-tysolin resistance family 266
Part 8: H+ -Dependent Symporters 272
Chapter 24. H+/sugar symporter-uniporter family 273
Chapter 25. H+/Rhamnose symporter family 299
Chapter 26. H+/amino acid symporter family 301
Chapter 27. H+/lactose-sucrose-nucleoside symporter family 312
Chapter 28. H+/galactoside-pentose-hexuronide symporter family 316
Chapter 29. H+/oligopeptide symporter family 321
Chapter 30. H+/fucose symporter family 328
Chapter 31. H+/carboxylate symporter family 331
Chapter 32. H+/nucleotide symporter family 337
Chapter 33. Sugar phosphate transporter family 340
Part 9: H+ -Dependent Antiporters 346
Chapter 34. H+/vesicular amine antiporter family 347
Chapter 35. 14-Helix H+/multidrug antiporter family 352
Chapter 36. 4-Helix H+/multidrug antiporter family 364
Chapter 37. 12-Helix H+/multidrug antiporter family 368
Chapter 38. Acriflavin-cation resistance family 375
Chapter 39. Yeast multidrug resistance family 381
Part 10: Na+ -Dependent Symporters 386
Chapter 40. Na+/Ca2+ exchanger family 387
Chapter 41. Na+/proline symporter family 391
Chapter 42. Na+/glucose symporter family 396
Chapter 43. Na+/dicarboxylate symporter family 403
Chapter 44. Na+PO4 symporter family 411
Chapter 45. Na+/branched amino acid symporter family 415
Chapter 46. Na+/citrate symporter family 419
Chapter 47. Na+/alanine-glycine symporter family 422
Chapter 48. Na+/neurotransmitter symporter family 425
Part 11: Na+ -Dependent Antiporters 438
Chapter 49. Na+/H+ antiporter family 439
Part 12: PEP-Dependent Phosphotransferase Family 446
Chapter 50. Phosphoenolpyruvate-dependent sugar phosphotransferase family 447
Part 13: Other Transporters 456
Chapter 51. Anion exchanger family 457
Chapter 52. Mitochondnal adenine nucleotide translocator family 465
Chapter 53. Mitochondrial phosphate carrier family 480
Chapter 54. Nitrate transporter I family 483
Chapter 55. Nitrate transporter II family 487
Chapter 56. Spore germination transporter family 490
Chapter 57. Vacuolar membrane pyrophosphatase family 493
Chapter 58. Gluconate transporter family 497
Index 503
Function and Structure of Membrane Transport Proteins
Peter J.F. Henderson (Department of Biochemistry and Molecular Biology, University of Leeds, Leeds LS2 9JT, UK)
INTRODUCTION
The hydrophobic bilayer membrane that bounds cells is inherently impermeable to the great majority of hydrophilic solutes required for cell nutrition and to many of the waste products and/or toxins that must be excreted. Accordingly, the membrane contains proteins, the sole function of which is to catalyze the translocation of substrates through the membrane. As the substrates for many membrane processes can be obtained in radioisotope-labeled form, it has been technically feasible to characterize the functions of many of these transport proteins. The structures of the proteins themselves, however, have proved to be difficult to elucidate: they are of low natural abundance in the membrane; they are very hydrophobic and refractory to isolation methods in aqueous solutions; and, even when purified, usually in non-denaturing detergents, they are very difficult to crystallize. Where the proteins happen to be abundant - bacteriorhodopsin from Halobacterium halobium, K+/Na+ ATPases in nerve and Ca2+ ATPase from muscle, cytochrome oxidases in bacteria and mitochondria, glucose transporter from human erythrocytes, for example – progress has been made in elucidating the structure–function relationship. Yet, of these proteins the three-dimensional structure has only been determined for bacteriorhodopsin and the oxidases1–3, and this is just the beginning of determining their molecular mechanisms of operation.
Free-living microorganisms (bacteria, algae, yeasts, parasitic protozoa) often inhabit environments where nutrients are in short supply, and different species must compete with each other for the available metabolites. Accordingly, they couple expenditure of metabolic energy to inward transport of essential nutrients (K+, NH+4, Pi, SO2−4, sugars, vitamins, etc.) to achieve intracellular concentrations sufficient for optimal growth rates. This expenditure can amount to 20–30% of the organism's available energy when a carbohydrate is fermented under anaerobic conditions to yield only 2–3 moles ATP per mole sugar4,5. Since the efficiencies of the transport steps may therefore influence cell yield and growth rate4,6,7 an understanding of the transport processes is important to both the academic researcher seeking to understand bacterial cell physiology, and the industrial manager trying to maintain the profitability of a fermentation process. Furthermore, the process of eliminating metabolic wastes and/or toxins such as antibiotics is often coupled to the expenditure of metabolic energy, an indication of its importance for survival. Motility appears to be driven by transport processes also, although this may not consume so much energy8.
In higher organisms, where survival functions are distributed between different organs, the energization of nutrient capture and waste efflux may be confined to specific tissues, e.g. the gut and the kidney. As a result of their activities, cells in other tissues enjoy an unchallenging environment in which their energy reserves can be channeled into other functions. Thus, their transport processes more often occur by facilitated diffusion.
As approximately 5–15% of all proteins, revealed by the current efforts in genome sequencing, are membrane transport proteins9, we anticipate the need for a huge effort in the new millennium to determine the structures of these proteins that are vital for the capture of nutrients and hence the first stage in cell growth. Their additional roles in antibiotic resistance, toxin secretion, ATP synthesis, ion balance, generation of action potentials, synaptic neurotransmission, kidney function, intestinal absorption, tumor growth and other diverse cell functions in organisms from microbe to man presage a major investigative effort to elucidate their molecular mechanisms of action. This effort to elucidate vectorial processes can be compared to the continuing efforts to understand enzyme-mediated catalysis, though there is the possibility of an underlying uniformity of translocation mechanism despite the huge numbers of independent transport proteins that exist.
The advent of recombinant DNA technology has enabled the study of membrane transport proteins to be furthered in at least four major directions. The first is the burgeoning appearance of an enormous number of amino acid sequences of the proteins predicted from the DNA sequences of their genes in the genome mapping projects. This sequence information has enabled a second advance: the unambivalent exposure of the evolutionary relationships between proteins not thought hitherto to be related. The third is the manipulation of the genes to expedite amplified expression and purification of the proteins. Finally the ability to mutagenize individual amino acids and to make chimeric proteins is being used to elucidate the relationship of function to structure.
A number of transport proteins play a role in human health and disease. The study of “ABC” transport systems (see later) in mammalian cells was intensified with the discovery that cystic fibrosis, the commonest inherited disease in the western world, was caused by a defect in the Cl− transport protein10. The significance of a multidrug resistance protein, “Mdr” that catalyzes secretion of cytotoxins and the failure of anti-tumor chemotherapy similarly focused attention on a different ABC system. In both cases their similarity as ABC-type systems would have been completely obscured without the amino acid sequence information derived from the cloning and sequencing of their genes. Other transport proteins are involved in glucose/galactose malabsorption, albinism, adrenoleukodystrophy.
This FactsBook is intended to catalyze this new age of exploration of membrane transport protein structure. It is our major goal to arrive at a sensible classification of transport systems based upon both evolutionary and mechanistic considerations. The numbers of protein sequences now known is too large to include them all, and the expected appearance of legions more from the genome sequencing programs makes it timely to formulate a systematic approach to their classification. First it is important to describe current concepts of their functions. The treatment below is necessarily brief, and the reader is referred to the appropriate chapters in standard biochemistry textbooks11,12 for a fuller introduction.
A watershed in the field occurred when Peter Mitchell13–15 showed that transport processes were intimately associated with the mechanism of oxidative and photosynthetic ATP synthesis, a process which is central to energy metabolism in almost all organisms. However, because of the difficulties in studying the hydrophobic membrane proteins involved we know very little about the molecular mechanism of such vectorial events; this contrasts with the wealth of information on the molecular mechanisms of chemical events catalyzed by water-soluble enzymes. It is quite possible that there is an underlying unity in the molecular mechanism of the translocation process, even when the direction of solute movement and any energization steps are completely different. This question is likely to be illuminated only when we elucidate the 3D structures and determine the structure-activity relationships of the transport proteins. By far the most central question in the transport field is precisely this – what are the 3D structures of the proteins involved?
Before reaching this question it is useful to define some terms often used in the characterization of transport processes.
USEFUL CONCEPTS
Passive diffusion
Passive diffusion is the translocation of a solute across a membrane down its electrochemical gradient without the participation of a transport protein. The process follows Fick's law, and so obeys the relationship below in which the velocity has a linear relationship to the [solute]:
=PAc
where v is velocity, P is the permeability coefficient for the particular solute, A is the area, and c is the difference in solute concentration across the cell membrane.
Diffusion has a low temperature coefficient (v ∝ absolute temperature) and is non-specific. Typical biologically important compounds that follow this mechanism are O2, CO2, NH3, HCO2H, CH3CO2H, CH2OH.CHOH.CH2OH – small, neutral molecules that are soluble in lipid membranes.
Facilitated diffusion
Facilitated diffusion is the translocation of a solute across a membrane down its electrochemical gradient catalyzed by a transport protein. The Michaelis–Menten relationship11,12 often adequately relates the initial rate of transport (v) to initial substrate concentration ([S] = c at zero time):
=Vmax.[S]/(Km+[S])
(Vmax is maximum velocity, Km = [S] where v is Vmax/2). As with enzyme reactions, there is a high temperature coefficient and, usually, strong substrate specificity. Biological substrates that follow this mechanism are typically charged and/or larger than about the size of glycerol, with a very low inherent solubility in biological membranes. Mitchell classified such transport of a single substrate as “uniport”, and glycerol transport is an example of...
Erscheint lt. Verlag | 22.12.1997 |
---|---|
Sprache | englisch |
Themenwelt | Naturwissenschaften ► Biologie ► Biochemie |
Naturwissenschaften ► Biologie ► Genetik / Molekularbiologie | |
Naturwissenschaften ► Biologie ► Zellbiologie | |
Naturwissenschaften ► Physik / Astronomie ► Angewandte Physik | |
Technik | |
ISBN-10 | 0-08-054265-4 / 0080542654 |
ISBN-13 | 978-0-08-054265-2 / 9780080542652 |
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