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Crystal structure of lpg1832, a VirK family protein from Legionella pneumophila , reveals a novel fold for bacterial VirK proteins
Author(s) -
Zhang Nannan,
Yin Shiyan,
Liu Shan,
Sun Aihong,
Zhou Mingxue,
Gong Xiaojian,
Ge Honghua
Publication year - 2017
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1002/1873-3468.12773
Subject(s) - homotetramer , legionella pneumophila , protein family , crystallography , chemistry , protein structure , protein crystallization , bacterial protein , crystal structure , biology , bacteria , biochemistry , genetics , crystallization , organic chemistry , protein subunit , gene
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, we determined the crystal structure of lpg1832, a VirK family protein from Legionella pneumophila , at 2.0 Å 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.