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Expression, purification, crystallization and crystallographic analysis of the N‐terminal domain of translocated intimin receptor
Author(s) -
Huang BingYang,
Gu Jiang,
Zhang YanFang,
Zhou JunJun,
Song XiaoYong,
Lin Yi,
Li XinMin,
Li Lu
Publication year - 2016
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.572
H-Index - 37
ISSN - 2053-230X
DOI - 10.1107/s2053230x15023274
Subject(s) - intimin , escherichia coli , biology , orthorhombic crystal system , intracellular , cytoplasm , crystallization , secretion , microbiology and biotechnology , bacterial outer membrane , signal transduction , chemistry , crystallography , biochemistry , enterobacteriaceae , gene , crystal structure , organic chemistry
Translocated intimin receptor (Tir) is an Escherichia coli ‐encoded protein that is transported into the host cell through a sophisticated bacterial type III secretion system (T3SS). Tir anchors the infected cell membrane twice using both its N‐ and C‐termini from inside the host cytoplasm for signalling. It plays a key role in enterohemorrhagic Escherichia coli (EHEC) infection, attaching and effacing (A/E) lesions and intracellular signal transduction. Here, the overexpression, purification and crystallization of its N‐terminal intracellular domain are reported. The crystal belonged to the orthorhombic space group I 4 1 22, with unit‐cell parameters a = b = 59.79, c = 183.11 Å. The asymmetric unit contained one molecule, with a solvent content of 51% and a V M of 2.55 Å 3 Da −1 .