1r1m
From Proteopedia
| Line 1: | Line 1: | ||
[[Image:1r1m.gif|left|200px]] | [[Image:1r1m.gif|left|200px]] | ||
| - | + | <!-- | |
| - | + | The line below this paragraph, containing "STRUCTURE_1r1m", creates the "Structure Box" on the page. | |
| - | + | You may change the PDB parameter (which sets the PDB file loaded into the applet) | |
| - | + | or the SCENE parameter (which sets the initial scene displayed when the page is loaded), | |
| - | | | + | or leave the SCENE parameter empty for the default display. |
| - | | | + | --> |
| - | + | {{STRUCTURE_1r1m| PDB=1r1m | SCENE= }} | |
| - | + | ||
| - | + | ||
| - | }} | + | |
'''Structure of the OmpA-like domain of RmpM from Neisseria meningitidis''' | '''Structure of the OmpA-like domain of RmpM from Neisseria meningitidis''' | ||
| Line 27: | Line 24: | ||
[[Category: Buchanan, S K.]] | [[Category: Buchanan, S K.]] | ||
[[Category: Grizot, S.]] | [[Category: Grizot, S.]] | ||
| - | [[Category: | + | [[Category: Membrane protein]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 06:57:56 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
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
