3SLU

Crystal structure of NMB0315

3SLU の概要

• エントリーDOI: 10.2210/pdb3slu/pdb
• 分子名称: M23 peptidase domain protein, NICKEL (II) ION (3 entities in total)
• 機能のキーワード: outer membrane, hydrolase
• 由来する生物種: Neisseria meningitidis
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 79776.41

構造登録者

Shen, Y.,Wang, X.,Yang, X.,Xu, H. (登録日: 2011-06-26, 公開日: 2012-02-01, 最終更新日: 2024-03-20)

主引用文献

Wang, X.,Yang, X.,Yang, C.,Wu, Z.,Xu, H.,Shen, Y.
Crystal structure of outer membrane protein NMB0315 from Neisseria meningitidis.
Plos One, 6:e26845-e26845, 2011

PubMed 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.

PubMed: 22046377
DOI: 10.1371/journal.pone.0026845

実験手法

X-RAY DIFFRACTION (2.41 Å)