Structural highlights
Publication Abstract from PubMed
VirK family [Pfam06903] consists of 14 bacterial VirK proteins of around 145 residues in length. The function of this family is unknown. Herein, using single-wavelength anomalous diffraction (SAD), we determined the crystal structure of lpg1832, a VirK family protein from Legionella pneumophila, at 2.0 A resolution. This is the first structural determination of a VirK domain-containing protein. Lpg1832 is a type II secretion system-dependent extracellular protein that folds into a novel barrel-shaped structure. It is found to adopt a quaternary assembly comprising a homotetramer. The three-dimensional structure of lpg1832 provides the first structural information pertaining to the VirK family and allows us to possibly identify its functionally important regions. This article is protected by copyright. All rights reserved.
Crystal structure of lpg1832, a VirK family protein from Legionella pneumophila, reveals a novel fold for bacterial VirK proteins.,Zhang N, Yin S, Liu S, Sun A, Zhou M, Gong X, Ge H FEBS Lett. 2017 Aug 3. doi: 10.1002/1873-3468.12773. PMID:28771688[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Zhang N, Yin S, Liu S, Sun A, Zhou M, Gong X, Ge H. Crystal structure of lpg1832, a VirK family protein from Legionella pneumophila, reveals a novel fold for bacterial VirK proteins. FEBS Lett. 2017 Aug 3. doi: 10.1002/1873-3468.12773. PMID:28771688 doi:http://dx.doi.org/10.1002/1873-3468.12773
