1R1M
Structure of the OmpA-like domain of RmpM from Neisseria meningitidis
Summary for 1R1M
| Entry DOI | 10.2210/pdb1r1m/pdb |
| Descriptor | Outer membrane protein class 4, 2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL (3 entities in total) |
| Functional Keywords | membrane protein |
| Biological source | Neisseria meningitidis |
| Cellular location | Cell outer membrane; Multi-pass membrane protein (By similarity): P38367 |
| Total number of polymer chains | 1 |
| Total formula weight | 18455.85 |
| Authors | Grizot, S.,Buchanan, S.K. (deposition date: 2003-09-24, release date: 2004-05-11, Last modification date: 2024-11-20) |
| Primary citation | Grizot, S.,Buchanan, S.K. Structure of the OmpA-like domain of RmpM from Neisseria meningitidis Mol.Microbiol., 51:1027-1037, 2004 Cited by PubMed Abstract: 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. PubMed: 14763978DOI: 10.1111/j.1365-2958.2003.03903.x PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.9 Å) |
Structure validation
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