2uyd: Difference between revisions

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[[Image:2uyd.jpg|left|200px]]
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[[Image:2uyd.png|left|200px]]


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{{STRUCTURE_2uyd|  PDB=2uyd  |  SCENE=  }}  
{{STRUCTURE_2uyd|  PDB=2uyd  |  SCENE=  }}  


'''CRYSTAL STRUCTURE OF THE SMHASA MUTANT H83A'''
===CRYSTAL STRUCTURE OF THE SMHASA MUTANT H83A===




==Overview==
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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.
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{{ABSTRACT_PUBMED_18162469}}


==About this Structure==
==About this Structure==
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[[Category: Metal-binding]]
[[Category: Metal-binding]]
[[Category: Metal-binding protein]]
[[Category: Metal-binding protein]]
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Revision as of 02:13, 29 July 2008

File:2uyd.png

Template:STRUCTURE 2uyd

CRYSTAL STRUCTURE OF THE SMHASA MUTANT H83A

Template:ABSTRACT PUBMED 18162469

About this Structure

2UYD is a Single protein structure of sequence from Serratia marcescens. 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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