3SLU

Crystal structure of NMB0315

Summary for 3SLU

• Entry DOI: 10.2210/pdb3slu/pdb
• Descriptor: M23 peptidase domain protein, NICKEL (II) ION (3 entities in total)
• Functional Keywords: outer membrane, hydrolase
• Biological source: Neisseria meningitidis
• Total number of polymer chains: 2
• Total formula weight: 79776.41

Authors

Shen, Y.,Wang, X.,Yang, X.,Xu, H. (deposition date: 2011-06-26, release date: 2012-02-01, Last modification date: 2024-03-20)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (2.41 Å)