1r1m
From Proteopedia
(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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| - | [[Image:1r1m.gif|left|200px]]<br /><applet load="1r1m" size=" | + | [[Image:1r1m.gif|left|200px]]<br /><applet load="1r1m" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1r1m, resolution 1.9Å" /> | caption="1r1m, resolution 1.9Å" /> | ||
'''Structure of the OmpA-like domain of RmpM from Neisseria meningitidis'''<br /> | '''Structure of the OmpA-like domain of RmpM from Neisseria meningitidis'''<br /> | ||
==Overview== | ==Overview== | ||
| - | RmpM is a putative peptidoglycan binding protein from Neisseria | + | 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== | ==About this Structure== | ||
| - | 1R1M is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Neisseria_meningitidis Neisseria meningitidis] with TRS as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | + | 1R1M is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Neisseria_meningitidis Neisseria meningitidis] with <scene name='pdbligand=TRS:'>TRS</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1R1M OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Neisseria meningitidis]] | [[Category: Neisseria meningitidis]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Buchanan, S | + | [[Category: Buchanan, S K.]] |
[[Category: Grizot, S.]] | [[Category: Grizot, S.]] | ||
[[Category: TRS]] | [[Category: TRS]] | ||
[[Category: membrane protein]] | [[Category: membrane protein]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:46:04 2008'' |
Revision as of 12:46, 21 February 2008
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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 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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