1r1m
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(New page: 200px<br /><applet load="1r1m" size="450" color="white" frame="true" align="right" spinBox="true" caption="1r1m, resolution 1.9Å" /> '''Structure of the OmpA...)
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Revision as of 23:04, 20 November 2007
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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 with TRS as ligand. 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
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