Skip to main content Accessibility help
×
Hostname: page-component-77c89778f8-cnmwb Total loading time: 0 Render date: 2024-07-19T15:35:27.902Z Has data issue: false hasContentIssue false
This chapter is part of a book that is no longer available to purchase from Cambridge Core

6 - Functions and Families

Mary Luckey
Affiliation:
San Francisco State University
Get access

Summary

The functions of most membrane proteins are traditionally described as enzymes, transporters and channels, and receptors, although the demarcations of these groups are blurred. For example, ATPases that are ion channels and other active transport proteins (“permeases”) are studied as enzymes as well as transporters. Some receptors involved in signaling are also tyrosine kinases; other receptors are gated ion channels. Membrane proteins can also be classified using data from bioinformatics, which describe families of proteins, functions of homologous domains, and evolutionary relationships. This chapter utilizes both approaches to look at the roles of membrane proteins before turning to tools for prediction of membrane protein structure and genomic analysis of membrane proteins. It starts by describing the general characteristics of membrane enzymes, transporters, and receptors, giving specific examples and briefly identifying their protein families.

MEMBRANE ENZYMES

The enzymes found in membranes carry out diverse covalent catalytic functions. In addition to solute transport and signaling, membrane-bound enzymes participate in electron transport chains and other redox reactions, as well as the metabolism of membrane components such as phospholipids and sterols. Many membrane enzymes require specific lipids or particular types of lipids for activity (see “Protein–Lipid Interactions” in Chapter 4). In addition, soluble enzymes may bind to the membrane periphery for catalysis involving substrates in the membrane, for efficient access to substrates that are passed along a series of bound enzymes to avoid dilution in the cytoplasm, or for regulation by modulation of their activities as described in Chapter 4.

Type
Chapter
Information
Membrane Structural Biology
With Biochemical and Biophysical Foundations
, pp. 127 - 159
Publisher: Cambridge University Press
Print publication year: 2008

Access options

Get access to the full version of this content by using one of the access options below. (Log in options will check for institutional or personal access. Content may require purchase if you do not have access.)

References

Li, H., and Poulos, T. L., Crystallization of cytochromes P450 and substrate–enzyme interactions. Curr Top Med Chem. 2004, 4:1789–1802.CrossRefGoogle ScholarPubMed
Carman, G. M., Deems, R. A., and Dennis, E. A., Lipid signaling enzymes and surface dilution kinetics. J Biol Chem. 1995, 270:18711–18714.CrossRefGoogle ScholarPubMed
Busch, W., and Saier, M. H. Jr., The transporter classification (TC) system, 2002. Crit Rev Biochem Mol Biol. 2002, 37:287–337.CrossRefGoogle ScholarPubMed
Saier, M. H. Jr., Families of transmembrane sugar transport proteins. Mol Microbiol. 2000, 35:699–710.CrossRefGoogle ScholarPubMed
Gruber, G., et al., Structure–function relationships of A-, F- and V-ATPases. J Exp Biol. 2001, 204:2597–2605.Google ScholarPubMed
Locher, K. P., Structure and mechanism of ABC transporters. Curr Opin Struct Biol. 2004, 14:426–431.CrossRefGoogle ScholarPubMed
Tchieu, J. H., et al., The complete phosphotransferase system in Escherichia coli. J Mol Microbiol Biotechnol. 2001, 3:329–346.Google ScholarPubMed
Kunji, E. R. S., The role and structure of mitochondrial carriers. FEBS Lett. 2004, 564:239–244.CrossRefGoogle ScholarPubMed
Pebay-Peyroula, E., and Brandolin, G., Nucleotide exchange in mitochrondria: insight at a molecular level. Curr Opin Struct Biol. 2004, 14:420–425.CrossRefGoogle Scholar
Miyazaya, A., et al., Nicotinic acetylcholine receptor at 4.6Å resolution. J Mol Biol. 1999, 288:765–786.CrossRefGoogle Scholar
Sixma, T. K., and Smit, A. B., Acetylcholine binding protein (AchBP)…pentameric ligand-gated ion channels. Annu Rev Biophys Biomol Struct. 2003, 32:311–334.CrossRefGoogle Scholar
Bockaert, J., and Pin, J. P., Molecular tinkering of G protein-coupled receptors: an evolutionary success. EMBO J. 1999, 18:1723–1729.CrossRefGoogle Scholar
Heijne, G., Membrane proteins from sequence to structure. Annu Rev Biophys Biomol Struct. 1994, 23:167–192.CrossRefGoogle Scholar
Heijne, G., Recent advances in the understanding of membrane protein assembly and structure. Q Rev Biophys. 1999, 4: 285–307.CrossRefGoogle Scholar
Tusnady, G. E., and Simon, I., Principles governing amino acid composition of integral membrane proteins: application to topology prediction. J Mol Biol. 1998, 283:489–506.CrossRefGoogle ScholarPubMed
Lehnert, U., et al., Computational analysis of membrane proteins: genomic occurrence, structure prediction and helix interactions. Q Rev Biophys. 2004, 37:121–146.CrossRefGoogle ScholarPubMed
Daley, D. O., et al., Global topology analysis of the Escherichia coli inner membrane proteome. Science. 2005, 308:1321–1323.CrossRefGoogle ScholarPubMed
Zhai, Y., and Saier, M. H. Jr., The β-barrel finder (BBF) program. Protein Sci. 2002, 11:2169–2207.Google ScholarPubMed
Wimley, W. C., Toward genomic identification of β-barrel membrane proteins, Protein Sci. 2002, 11:301–312.CrossRefGoogle ScholarPubMed
Adamian, L., et al., Higher-order interhelical spatial interactions in membrane proteins. J Mol Biol. 2003, 327:251–272.CrossRefGoogle ScholarPubMed
Stenberg, F., et al., Protein complexes of the Escherichia coli cell envelope. J Biol Chem. 2005, 280:34409–34419.CrossRefGoogle ScholarPubMed
Li, H., and Poulos, T. L., Crystallization of cytochromes P450 and substrate–enzyme interactions. Curr Top Med Chem. 2004, 4:1789–1802.CrossRefGoogle ScholarPubMed
Carman, G. M., Deems, R. A., and Dennis, E. A., Lipid signaling enzymes and surface dilution kinetics. J Biol Chem. 1995, 270:18711–18714.CrossRefGoogle ScholarPubMed
Busch, W., and Saier, M. H. Jr., The transporter classification (TC) system, 2002. Crit Rev Biochem Mol Biol. 2002, 37:287–337.CrossRefGoogle ScholarPubMed
Saier, M. H. Jr., Families of transmembrane sugar transport proteins. Mol Microbiol. 2000, 35:699–710.CrossRefGoogle ScholarPubMed
Gruber, G., et al., Structure–function relationships of A-, F- and V-ATPases. J Exp Biol. 2001, 204:2597–2605.Google ScholarPubMed
Locher, K. P., Structure and mechanism of ABC transporters. Curr Opin Struct Biol. 2004, 14:426–431.CrossRefGoogle ScholarPubMed
Tchieu, J. H., et al., The complete phosphotransferase system in Escherichia coli. J Mol Microbiol Biotechnol. 2001, 3:329–346.Google ScholarPubMed
Kunji, E. R. S., The role and structure of mitochondrial carriers. FEBS Lett. 2004, 564:239–244.CrossRefGoogle ScholarPubMed
Pebay-Peyroula, E., and Brandolin, G., Nucleotide exchange in mitochrondria: insight at a molecular level. Curr Opin Struct Biol. 2004, 14:420–425.CrossRefGoogle Scholar
Miyazaya, A., et al., Nicotinic acetylcholine receptor at 4.6Å resolution. J Mol Biol. 1999, 288:765–786.CrossRefGoogle Scholar
Sixma, T. K., and Smit, A. B., Acetylcholine binding protein (AchBP)…pentameric ligand-gated ion channels. Annu Rev Biophys Biomol Struct. 2003, 32:311–334.CrossRefGoogle Scholar
Bockaert, J., and Pin, J. P., Molecular tinkering of G protein-coupled receptors: an evolutionary success. EMBO J. 1999, 18:1723–1729.CrossRefGoogle Scholar
Heijne, G., Membrane proteins from sequence to structure. Annu Rev Biophys Biomol Struct. 1994, 23:167–192.CrossRefGoogle Scholar
Heijne, G., Recent advances in the understanding of membrane protein assembly and structure. Q Rev Biophys. 1999, 4: 285–307.CrossRefGoogle Scholar
Tusnady, G. E., and Simon, I., Principles governing amino acid composition of integral membrane proteins: application to topology prediction. J Mol Biol. 1998, 283:489–506.CrossRefGoogle ScholarPubMed
Lehnert, U., et al., Computational analysis of membrane proteins: genomic occurrence, structure prediction and helix interactions. Q Rev Biophys. 2004, 37:121–146.CrossRefGoogle ScholarPubMed
Daley, D. O., et al., Global topology analysis of the Escherichia coli inner membrane proteome. Science. 2005, 308:1321–1323.CrossRefGoogle ScholarPubMed
Zhai, Y., and Saier, M. H. Jr., The β-barrel finder (BBF) program. Protein Sci. 2002, 11:2169–2207.Google ScholarPubMed
Wimley, W. C., Toward genomic identification of β-barrel membrane proteins, Protein Sci. 2002, 11:301–312.CrossRefGoogle ScholarPubMed
Adamian, L., et al., Higher-order interhelical spatial interactions in membrane proteins. J Mol Biol. 2003, 327:251–272.CrossRefGoogle ScholarPubMed
Stenberg, F., et al., Protein complexes of the Escherichia coli cell envelope. J Biol Chem. 2005, 280:34409–34419.CrossRefGoogle ScholarPubMed

Save book to Kindle

To save this book to your Kindle, first ensure coreplatform@cambridge.org is added to your Approved Personal Document E-mail List under your Personal Document Settings on the Manage Your Content and Devices page of your Amazon account. Then enter the ‘name’ part of your Kindle email address below. Find out more about saving to your Kindle.

Note you can select to save to either the @free.kindle.com or @kindle.com variations. ‘@free.kindle.com’ emails are free but can only be saved to your device when it is connected to wi-fi. ‘@kindle.com’ emails can be delivered even when you are not connected to wi-fi, but note that service fees apply.

Find out more about the Kindle Personal Document Service.

  • Functions and Families
  • Mary Luckey, San Francisco State University
  • Book: Membrane Structural Biology
  • Online publication: 05 June 2012
  • Chapter DOI: https://doi.org/10.1017/CBO9780511811098.007
Available formats
×

Save book to Dropbox

To save content items to your account, please confirm that you agree to abide by our usage policies. If this is the first time you use this feature, you will be asked to authorise Cambridge Core to connect with your account. Find out more about saving content to Dropbox.

  • Functions and Families
  • Mary Luckey, San Francisco State University
  • Book: Membrane Structural Biology
  • Online publication: 05 June 2012
  • Chapter DOI: https://doi.org/10.1017/CBO9780511811098.007
Available formats
×

Save book to Google Drive

To save content items to your account, please confirm that you agree to abide by our usage policies. If this is the first time you use this feature, you will be asked to authorise Cambridge Core to connect with your account. Find out more about saving content to Google Drive.

  • Functions and Families
  • Mary Luckey, San Francisco State University
  • Book: Membrane Structural Biology
  • Online publication: 05 June 2012
  • Chapter DOI: https://doi.org/10.1017/CBO9780511811098.007
Available formats
×