3slu | pdb_00003slu

Crystal structure of NMB0315

spinqualitylabelsall models 3slu, resolution 2.41Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3slu is a 2 chain structure with sequence from Neisseria meningitidis atcc 13091. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: NI Gene: HMPREF0602_0018 (Neisseria meningitidis ATCC 13091) Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed NMB0315 is an outer membrane protein of Neisseria meningitidis serogroup B (NMB) and a potential candidate for a broad-spectrum vaccine against meningococcal disease. The crystal structure of NMB0315 was solved by single-wavelength anomalous dispersion (SAD) at a resolution of 2.4 A and revealed to be a lysostaphin-type peptidase of the M23 metallopeptidase family. The overall structure consists of three well-separated domains and has no similarity to any previously published structure. However, only the topology of the carboxyl-terminal domain is highly conserved among members of this family, and this domain is a zinc-dependent catalytic unit. The amino-terminal domain of the structure blocks the substrate binding pocket in the carboxyl-terminal domain, indicating that the wild-type full-length protein is in an inactive conformational state. Our studies improve the understanding of the catalytic mechanism of M23 metallopeptidases. Crystal structure of outer membrane protein NMB0315 from Neisseria meningitidis.,Wang X, Yang X, Yang C, Wu Z, Xu H, Shen Y PLoS One. 2011;6(10):e26845. Epub 2011 Oct 26. PMID:22046377 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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