title: Crystal structure of outer membrane protein NMB0315 from Neisseria meningitidis.
abstract: 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 Å 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.
authors: State Key Laboratory of Medicinal Chemical Biology, Nankai University, Tianjin, China.
authors: Xiangyu
authors: X
authors: Wang
authors: Xue
authors: X
authors: Yang
authors: Chunting
authors: C
authors: Yang
authors: Zhenhua
authors: Z
authors: Wu
authors: Honglin
authors: H
authors: Xu
authors: Yuequan
authors: Y
authors: Shen
mesh_terms: D000595:Amino Acid Sequence; D001425:Bacterial Outer Membrane Proteins / Q000737:chemistry*; D001665:Binding Sites; D055162:Biocatalysis; D018360:Crystallography, X-Ray; D045726:Metalloproteases; D008958:Models, Molecular; D008969:Molecular Sequence Data; D009345:Neisseria meningitidis / Q000737:chemistry*; D038541:Neisseria meningitidis, Serogroup B; D017434:Protein Structure, Tertiary; D016415:Sequence Alignment; D040681:Structural Homology, Protein; D015032:Zinc
chemical_list: D001425:Bacterial Outer Membrane Proteins; D045726:Metalloproteases; D015032:Zinc