1887

Chapter 4 : Structure of Outer Membrane Receptor Proteins

MyBook is a cheap paperback edition of the original book and will be sold at uniform, low price.

Ebook: Choose a downloadable PDF or ePub file. Chapter is a downloadable PDF file. File must be downloaded within 48 hours of purchase

Buy this Chapter
Digital (?) $15.00

Preview this chapter:
Zoom in
Zoomout

Structure of Outer Membrane Receptor Proteins, Page 1 of 2

| /docserver/preview/fulltext/10.1128/9781555816544/9781555812928_Chap04-1.gif /docserver/preview/fulltext/10.1128/9781555816544/9781555812928_Chap04-2.gif

Abstract:

The outer membrane receptor proteins for ferric siderophores are physically similar to porins, being less hydrophobic than most other membrane proteins. This chapter discusses functions of outer membrane receptor proteins in the transport of ferric siderophores. The discussions are based on comparisons of the crystal structures of three of the proteins and on the simultaneous sequence alignment of many TonB-dependent proteins. The topics involve binding of substrate, signaling to the TonB box, interaction(s) with TonB, and effects of activated TonB on the structure of the outer membrane receptor protein. In addition, the chapter presents the organization of the globular domain, and the principle of bipartite gating. At various points, suggestions were put forward for new structural determinations. There are established methods to produce, purify, crystallize, and solve the structures of members of this family of proteins. This is applicable to newly identified members of this family and possibly to hybrid proteins and protein domains. Furthermore, the structural determination of a mutant protein or proteins with other small molecular changes is a much easier task than for new structures, because the time-consuming phase problem does not have to be solved. Instead, the intensity data of the mutant can be combined with the phases of the parent protein to obtain the initial structure, decreasing the required time from months to days for this task.

Citation: van der Helm D. 2004. Structure of Outer Membrane Receptor Proteins, p 51-65. In Crosa J, Mey A, Payne S, Iron Transport in Bacteria. ASM Press, Washington, DC. doi: 10.1128/9781555816544.ch4

Key Concept Ranking

Outer Membrane Proteins
0.54507935
0.54507935
Highlighted Text: Show | Hide
Loading full text...

Full text loading...

References

/content/book/10.1128/9781555816544.chap4
1. Barnard, T. J.,, M. E. Watson, Jr.,, and M. A. Mc- Intosh. 2001. Mutations in the Escherichia coli receptor FepA reveal residues involved in ligand binding and transport. Mol. Microbiol. 41: 527536.
2. Braun, M.,, H. Killmann,, and V. Braun. 1999. The beta-barrel domain of FhuA Δ5-160 is sufficient for TonB-dependent FhuA activities of Escherichia coli. Mol. Microbiol. 33: 10371049.
3. Buchanan, S. K.,, B. S. Smith,, L. Venkatramani,, D. Xia,, L. Esser,, M. Palnitkar,, R. Chakraborty,, D. van der Helm,, and J. Deisenhofer. 1999. Crystal structure of the outer membrane active transporter FepA from Escherichia coli. Nat. Struct. Biol. 6:5663.
4. Chakraborty, R.,, E. A. Lemke,, Z. Cao,, P. E. Klebba,, and D. van der Helm. 2003. Identification and mutational studies of conserved amino acids in the outer membrane receptor protein, FepA, which affect transport but not binding of ferric enterobactin in Escherichia coli. Biometals 16:507518.
5. Chimento, D. P.,, A. K. Mohanty,, R. J. Kadner, and M. C. Wiener. 2003. Substrate-induced transmembrane signaling in the cobalamin transporter BtuB. Nat. Struct. Biol. 10:394401.
6. Coulton, J. W.,, P. Mason,, D. R. Cameron,, G. Carmel,, R. Jean,, and H. N. Rode., 1986. Protein fusions of β-galactosidase to the ferrichrome-iron receptor of Escherichia coli K-12. J. Bacteriol. 165:181192.
7. Ferguson, A. D.,, E. Hofmann,, J. W. Coulton,, K. Diederichs,, and W. Welte. 1998. Siderophore-mediated iron transport: crystal structure of FhuA with bound lipopolysaccharide. Science 282: 22152220.
8. Ferguson, A. D.,, J. Ködding,, G. Walker,, C. Bös,, J. W. Coulton,, K. Diederichs,, V. Braun,, and W. Welte. 2001. Active transport of an antibiotic rifamycin derivative by the outer membrane protein FhuA. Structure 9:707716.
9. Ferguson, A. D.,, J. W. Coulton,, K. Diederichs,, and W. Welte,. 2001. The ferric hydroxamate uptake receptor FhuA and related TonB-dependent transporters in the outer membrane of gram-negative bacteria, p. 834849. In A. Messerschmidt,, R. Huber,, T. Poulos,, and K. Wieghardt (ed.), Handbook of Metalloproteins. John Wiley & Sons, Ltd., Chichester, United Kingdom.
10. Ferguson, A. D.,, R. Chakraborty,, B. S. Smith,, L. Esser,, D. van der Helm,, and J. Deisenhofer. 2002. Structural basis of gating by the outer membrane transporter FecA. Science 295:17151719.
11. Ferguson, A. D.,, V. Braun,, H.-P. Fiedler,, J. W. Coulton. K. Diederichs, and W. Welte. 2000. Crystal structure of the antibiotic albomycin in complex with the outer membrane transporter FhuA. Protein Sci. 9:956963.
12. Jalal, M. A. F.,, and D. van der Helm. 1989. Purification and crystallization of ferric enterobactin receptor protein, FepA, from the outer membranes of Escherichia coli UT5600/pBB2. FEBS Lett. 243: 366370.
13. Locher, K. P.,, B. Rees,, R. Koebnik,, A. Mitschler,, L. Moulinier,, J. P. Rosenbusch,, and D. Moras. 1998. Transmembrane signaling across the ligand-gated FhuA receptor: crystal structures of free and ferrichrome-bound states reveal allosteric changes. Cell 95:771778.
14. Lundrigan, M. D.,, and R. J. Kadner. 1986. Nucleotide sequence of the gene for the ferricenterochelin receptor FepA in Escherichia coli. J. Biol. Chem. 261: 1079710801.
15. Pressler, U.,, H. Staudenmaier,, L. Zimmermann,, and V. Braun. 1988. Genetics of the iron dicitrate transport system of Escherichia coli. J. Bacteriol. 170: 27162724.
16. Scott, D. C.,, Z. Cao,. Z. Qi,, M. Bauler,, J. D. Igo,, S. M. C. Newton,, and P. E. Klebba. 2001. Exchangeability of N termini in the ligand-gated porins of Escherichia coli. J. Biol. Chem. 276: 1302513033.
17. Smith, B. S.,, B. Kobe,, R. Kurumbail,, S. K. Buchanan,, L. Venkatramani,, D. vanderHelm,, and J. Deisenhofer. 1998. Crystallization and preliminary X-ray analysis of ferric enterobactin receptor FepA, an integral membrane protein from Escherichia coli. Acta Crystallogr. Sar. D 54:697699.
18. Vakharia, H. L.,, and K. Postle. 2002. FepA with globular domain deletions lacks activity. J. Bacteriol. 184:55085512.
19. van der Helm, D.,, and R. Chakraborty,. 2001. Structures of siderophore receptors, p. 261287. In G. Winkelmann (ed.), Microbial Transport Systems, Wiley-VCH, Weinheim, Germany.
20. van der Helm, D.,, R. Chakraborty,, A. D. Ferguson,, B. S. Smith,, L. Esser,, and J. Deisenhofer. 2002. Bipartite gating in the outer membrane protein FecA. Biochem. Soc. Trans. 30:708710.
21. van der Helm, D., 1998. The physical chemistry of bacterial outer membrane siderophore receptor proteins, p. 355401. In A. Sigel, and H. Sigel (ed.), Metal Ions in Biological Systems, vol. 35. Marcel Dekker, New York, N.Y.

Tables

Generic image for table
TABLE 1

Topologies of the globular domain in FecA, FhuA and FepA

Citation: van der Helm D. 2004. Structure of Outer Membrane Receptor Proteins, p 51-65. In Crosa J, Mey A, Payne S, Iron Transport in Bacteria. ASM Press, Washington, DC. doi: 10.1128/9781555816544.ch4

This is a required field
Please enter a valid email address
Please check the format of the address you have entered.
Approval was a Success
Invalid data
An Error Occurred
Approval was partially successful, following selected items could not be processed due to error