原创力文档crystal structure of outer membrane protein nmb0315 from neisseria meningitidis外膜蛋白的晶体结构nmb0315脑膜炎奈瑟菌.pdfVIP
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crystal structure of outer membrane protein nmb0315 from neisseria meningitidis外膜蛋白的晶体结构nmb0315脑膜炎奈瑟菌
Crystal Structure of Outer Membrane Protein NMB0315
from Neisseria meningitidis
1,2 1,2 3 3 3 1,2
Xiangyu Wang , Xue Yang , Chunting Yang , Zhenhua Wu , Honglin Xu *, Yuequan Shen *
1 State Key Laboratory of Medicinal Chemical Biology, Nankai University, Tianjin, China, 2 College of Life Sciences, Nankai University, Tianjin, China, 3 Laboratory of
Virology, National Vaccine and Serum Institute, Beijing, China
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 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.
Citation: Wang X, Yang X, Yang C, Wu Z, Xu H, et al. (2011) Crystal Structure of Outer Membrane Protein NMB0315 from Neisseria meningitidis. P
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