5XTA

Crystal structure of lpg1832, a VirK family protein from Legionella pneumophila

Summary for 5XTA

• Entry DOI: 10.2210/pdb5xta/pdb
• Descriptor: VirK protein, SULFATE ION, GLYCEROL, ... (4 entities in total)
• Functional Keywords: novel fold, type ii secretion, oxidoreductase
• Biological source: Legionella pneumophila
• Total number of polymer chains: 4
• Total formula weight: 53441.88

Authors

Yin, S.,Gong, X.,Zhang, N.,Ge, H. (deposition date: 2017-06-18, release date: 2017-08-16, Last modification date: 2024-10-16)

Primary citation

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., 591:2929-2935, 2017

PubMed Abstract: 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.

PubMed: 28771688
DOI: 10.1002/1873-3468.12773

Experimental method

X-RAY DIFFRACTION (2 Å)