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2uyd
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(New page: 200px<br /><applet load="2uyd" size="350" color="white" frame="true" align="right" spinBox="true" caption="2uyd, resolution 2.70Å" /> '''CRYSTAL STRUCTURE OF...)
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Revision as of 09:13, 23 January 2008
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CRYSTAL STRUCTURE OF THE SMHASA MUTANT H83A
Overview
Heme carrier HasA has a unique type of histidine/tyrosine heme iron, ligation in which the iron ion is in a thermally driven two spin state, equilibrium. We recently suggested that the H-bonding between Y75 and the, invariantly conserved residue H83 modulates the strength of the Fe-Y75, bond. To unravel the role of H83, we characterize the iron ligation and, the electronic properties of both wild type and H83A mutant by a variety, of spectroscopic techniques. While H83 in wild type modulates the strength, of the Tyr-iron bond, its removal causes detachment of the tyrosine, ligand, thus giving rise to a series of pH dependent equilibria among, species with different axial ligation. The five coordinated species, detected at physiological pH may represent a possible intermediate of the, heme transfer mechanism to the receptor.
About this Structure
2UYD is a Single protein structure of sequence from Serratia marcescens with , and as ligands. Known structural/functional Sites: , , , , , , , , and . Full crystallographic information is available from OCA.
Reference
Deciphering the structural role of histidine 83 for heme binding in hemophore HasA., Caillet-Saguy C, Turano P, Piccioli M, Lukat-Rodgers GS, Czjzek M, Guigliarelli B, Izadi-Pruneyre N, Rodgers KR, Delepierre M, Lecroisey A, J Biol Chem. 2007 Dec 27;. PMID:18162469
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