Crystal structure of outer membrane protein NMB0315 from Neisseria meningitidis |
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Authors: | Wang Xiangyu Yang Xue Yang Chunting Wu Zhenhua Xu Honglin Shen Yuequan |
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Affiliation: | State Key Laboratory of Medicinal Chemical Biology, Nankai University, Tianjin, China. |
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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. |
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