Open AccessCrystallization and preliminary X‐ray diffraction analysis of the haem‐binding protein HemS from Yersinia enterocolitica
Author(s) -
Schneider Sabine,
Paoli Massimo
Publication year - 2005
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309105023523
Subject(s) - yersinia enterocolitica , orthorhombic crystal system , crystallography , crystallization , chemistry , cytosol , biochemistry , biology , bacteria , crystal structure , enzyme , genetics , organic chemistry
Bacteria have evolved strategies to acquire iron from their environment. Pathogenic microbes rely on specialized proteins to `steal' haem from their host and use it as an iron source. HemS is the ultimate recipient of a molecular‐relay system for haem uptake in Gram‐negative species, functioning as the cytosolic carrier of haem. Soluble expression and high‐quality diffraction crystals were obtained for HemS from Yersinia enterocolitica . Crystals belong to the orthorhombic space group I 222, with unit‐cell parameters a = 74.86, b = 77.45, c = 114.09 Å, and diffract X‐rays to 2.6 Å spacing in‐house. Determination of the structure of the haem–HemS complex will reveal the molecular basis of haem binding.