Structural highlights
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Wang X, Yang X, Yang C, Wu Z, Xu H, Shen Y. Crystal structure of outer membrane protein NMB0315 from Neisseria meningitidis. PLoS One. 2011;6(10):e26845. Epub 2011 Oct 26. PMID:22046377 doi:10.1371/journal.pone.0026845
