Crystallization and preliminary X-ray diffraction analysis of the haem-binding protein HemS from Yersinia enterocolitica.
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.
Schneider
Sabine
S
Centre for Biomolecular Sciences, School of Pharmacy, University of Nottingham, University Park, Nottingham NG7 2RD, England.
Paoli
Massimo
M
D001426:Bacterial Proteins / Q000737:chemistry* / Q000302:isolation & purification; D002352:Carrier Proteins / Q000737:chemistry* / Q000302:isolation & purification; D003460:Crystallization; D004591:Electrophoresis, Polyacrylamide Gel; D000081062:Heme-Binding Proteins; D006420:Hemeproteins / Q000737:chemistry* / Q000302:isolation & purification; D026901:Membrane Transport Proteins / Q000737:chemistry* / Q000302:isolation & purification; D010088:Oxidoreductases / Q000737:chemistry* / Q000302:isolation & purification; D011993:Recombinant Fusion Proteins / Q000737:chemistry; D014961:X-Ray Diffraction; D015008:Yersinia enterocolitica / Q000737:chemistry*
D001426:Bacterial Proteins; D002352:Carrier Proteins; C090995:HemS protein, Yersinia enterocolitica; D000081062:Heme-Binding Proteins; D006420:Hemeproteins; D026901:Membrane Transport Proteins; D011993:Recombinant Fusion Proteins; D010088:Oxidoreductases