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spinqualitylabelsall models 2j0p, resolution 1.70Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

STRUCTURE OF THE HAEM-CHAPERONE PROTEOBACTERIA-PROTEIN HEMS

Overview

Bacteria rely on their environment and/or host to acquire iron and have, evolved specialized systems to sequester and transport heme. The heme, uptake system HemRSTUV is common to proteobacteria, and a major challenge, is to understand the molecular mechanism of heme binding and transfer, between the protein molecules that underlie this heme transport relay, process. In the Gram-negative pathogen Yersinia enterocolitica, the, HemRSTUV system culminates with the cytoplasmic recipient HemS, which, stores and delivers heme for cellular needs. HemS belongs to a family of, proteins essential and unique to proteobacteria. Here we report on the, binding mechanism of HemS based on structural data from its apo- and, ligand-loaded forms. This heme carrier protein associates with its cargo, through ... [(full description)]

About this Structure

2J0P is a [Single protein] structure of sequence from [Yersinia enterocolitica] with HEM, 12P, MLI and PEG as [ligands]. Structure known Active Site: AC1. Full crystallographic information is available from [OCA].

Reference

An induced fit conformational change underlies the binding mechanism of the heme transport proteobacteria-protein HemS., Schneider S, Sharp KH, Barker PD, Paoli M, J Biol Chem. 2006 Oct 27;281(43):32606-10. Epub 2006 Aug 30. PMID:16943192

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