Chapter 4 : Structure of Outer Membrane Receptor Proteins

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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
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Generic image for table

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

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