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1r1m
From Proteopedia
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|ACTIVITY= | |ACTIVITY= | ||
|GENE= RMPM ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=487 Neisseria meningitidis]) | |GENE= RMPM ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=487 Neisseria meningitidis]) | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1r1m FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1r1m OCA], [http://www.ebi.ac.uk/pdbsum/1r1m PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1r1m RCSB]</span> | ||
}} | }} | ||
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[[Category: Buchanan, S K.]] | [[Category: Buchanan, S K.]] | ||
[[Category: Grizot, S.]] | [[Category: Grizot, S.]] | ||
| - | [[Category: TRS]] | ||
[[Category: membrane protein]] | [[Category: membrane protein]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 23:21:57 2008'' |
Revision as of 20:21, 30 March 2008
| |||||||
| , resolution 1.9Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | |||||||
| Gene: | RMPM (Neisseria meningitidis) | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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 Sun Mar 30 23:21:57 2008
