2uyd
From Proteopedia
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| , resolution 2.70Å | |||||||
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| Sites: | , , , , , , , , and | ||||||
| Ligands: | , , | ||||||
| Related: | 1B2V, 1DK0, 1DKH, 1YBJ, 2CN4
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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. 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
Page seeded by OCA on Mon Mar 31 05:06:15 2008
