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1r1m
From Proteopedia
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'''Structure of the OmpA-like domain of RmpM from Neisseria meningitidis''' | '''Structure of the OmpA-like domain of RmpM from Neisseria meningitidis''' | ||
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[[Category: Buchanan, S K.]] | [[Category: Buchanan, S K.]] | ||
[[Category: Grizot, S.]] | [[Category: Grizot, S.]] | ||
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| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 06:57:56 2008'' | |
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Revision as of 03:57, 3 May 2008
Structure of the OmpA-like domain of RmpM from Neisseria meningitidis
Overview
RmpM is a putative peptidoglycan binding protein from Neisseria meningitidis that has been shown to interact with integral outer membrane proteins such as porins and TonB-dependent transporters. Here we report the 1.9 A crystal structure of the C-terminal domain of RmpM. The 150-residue domain adopts a betaalphabetaalphabetabeta fold, as first identified in Bacillus subtilis chorismate mutase. The C-terminal RmpM domain is homologous to the periplasmic, C-terminal domain of Escherichia coli OmpA; these domains are thought to be responsible for non-covalent interactions with peptidoglycan. From the structure of the OmpA-like domain of RmpM, we suggest a putative peptidoglycan binding site and identify residues that may be essential for binding. Both the crystal structure and solution experiments indicate that RmpM may exist as a dimer. This would promote more efficient peptidoglycan binding, by allowing RmpM to interact simultaneously with two glycan chains through its C-terminal, OmpA-like binding domain, while its (structurally uncharacterized) N-terminal domain could stabilize oligomers of porins and TonB-dependent transporters in the outer membrane.
About this Structure
1R1M is a Single protein structure of sequence from Neisseria meningitidis. Full crystallographic information is available from OCA.
Reference
Structure of the OmpA-like domain of RmpM from Neisseria meningitidis., Grizot S, Buchanan SK, Mol Microbiol. 2004 Feb;51(4):1027-37. PMID:14763978 Page seeded by OCA on Sat May 3 06:57:56 2008
