Literature DB >> 31706575

Crystal structure of a hypothetical T2SS effector Lpg0189 from Legionella pneumophila reveals a novel protein fold.

Xiaofang Chen1, Shan Liu2, Sha Jiang3, Xuecheng Zhang3, Nannan Zhang4, Jinming Ma5, Honghua Ge6.   

Abstract

Lpg0189 is a type II secretion system-dependent extracellular protein with unknown function from Legionella pneumophila. Herein, we determined the crystal structure of Lpg0189 at 1.98 Å resolution by using single-wavelength anomalous diffraction (SAD). Lpg0189 folds into a novel chair-shaped architecture, with two sheets roughly perpendicular to each other. Bioinformatics analysis suggests Lpg0189 and its homologues are unique to Legionellales and evolved divergently. The interlinking structural and bioinformatics studies provide a better understanding of this hypothetical protein.
Copyright © 2019 Elsevier Inc. All rights reserved.

Entities:  

Keywords:  Legionella pneumophila, novel fold; Lpg0189; Type II secretion

Year:  2019        PMID: 31706575     DOI: 10.1016/j.bbrc.2019.10.195

Source DB:  PubMed          Journal:  Biochem Biophys Res Commun        ISSN: 0006-291X            Impact factor:   3.575


  1 in total

1.  Structure, Dynamics and Cellular Insight Into Novel Substrates of the Legionella pneumophila Type II Secretion System.

Authors:  Theo J Portlock; Jessica Y Tyson; Sarath C Dantu; Saima Rehman; Richard C White; Ian E McIntire; Lee Sewell; Katherine Richardson; Rosie Shaw; Alessandro Pandini; Nicholas P Cianciotto; James A Garnett
Journal:  Front Mol Biosci       Date:  2020-06-11
  1 in total

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