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Crystallization and preliminary X-ray diffraction analysis of the haem-binding protein HemS from Yersinia enterocolitica.

ABSTRACT: 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 I222, with unit-cell parameters a = 74.86, b = 77.45, c = 114.09 A, and diffract X-rays to 2.6 A spacing in-house. Determination of the structure of the haem-HemS complex will reveal the molecular basis of haem binding.

SUBMITTER: Schneider S

PROVIDER: S-EPMC1952356 | biostudies-literature | 2005 Aug

REPOSITORIES: biostudies-literature

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Crystallization and preliminary X-ray diffraction analysis of the haem-binding protein HemS from Yersinia enterocolitica.

Schneider Sabine S Paoli Massimo M

Acta crystallographica. Section F, Structural biology and crystallization communications 20050730 Pt 8

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 I222, with ...[more]

PMID: 16511163

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