2cn4
From Proteopedia
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[[Category: transport protein]] | [[Category: transport protein]] | ||
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Revision as of 08:04, 30 October 2007
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THE CRYSTAL STRUCTURE OF THE SECRETED DIMERIC FORM OF THE HEMOPHORE HASA REVEALS A DOMAIN SWAPPING WITH AN EXCHANGED HEME LIGAND
Overview
To satisfy their iron needs, several Gram-negative bacteria use a heme, uptake system involving an extracellular heme-binding protein called, hemophore. The function of the hemophore is to acquire free or, hemoprotein-bound heme and to transfer it to HasR, its specific outer, membrane receptor, by protein-protein interaction. The hemophore HasA, secreted by Serratia marcescens, an opportunistic pathogen, was the first, to be identified and is now very well characterized. HasA is a monomer, that binds one b heme with strong affinity. The heme in HasA is highly, exposed to solvent and coordinated by an unusual pair of ligands, a, histidine and a tyrosine. Here, we report the identification, the, characterization and the X-ray structure of a dimeric form of HasA from S., marcescens: DHasA. ... [(full description)]
About this Structure
2CN4 is a [Single protein] structure of sequence from [Serratia marcescens] with PO4 and HEM as [ligands]. Structure known Active Site: HEM. Full crystallographic information is available from [OCA].
Reference
The crystal structure of the secreted dimeric form of the hemophore HasA reveals a domain swapping with an exchanged heme ligand., Czjzek M, Letoffe S, Wandersman C, Delepierre M, Lecroisey A, Izadi-Pruneyre N, J Mol Biol. 2007 Jan 26;365(4):1176-86. Epub 2006 Oct 25. PMID:17113104
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