2uyd
From Proteopedia
Line 1: | Line 1: | ||
[[Image:2uyd.jpg|left|200px]] | [[Image:2uyd.jpg|left|200px]] | ||
- | + | <!-- | |
- | + | The line below this paragraph, containing "STRUCTURE_2uyd", creates the "Structure Box" on the page. | |
- | + | You may change the PDB parameter (which sets the PDB file loaded into the applet) | |
- | + | or the SCENE parameter (which sets the initial scene displayed when the page is loaded), | |
- | + | or leave the SCENE parameter empty for the default display. | |
- | + | --> | |
- | | | + | {{STRUCTURE_2uyd| PDB=2uyd | SCENE= }} |
- | | | + | |
- | + | ||
- | }} | + | |
'''CRYSTAL STRUCTURE OF THE SMHASA MUTANT H83A''' | '''CRYSTAL STRUCTURE OF THE SMHASA MUTANT H83A''' | ||
Line 31: | Line 28: | ||
[[Category: Izadi-Pruneyre, N.]] | [[Category: Izadi-Pruneyre, N.]] | ||
[[Category: Lecroisey, A.]] | [[Category: Lecroisey, A.]] | ||
- | [[Category: | + | [[Category: Heme]] |
- | [[Category: | + | [[Category: Heme acquisition system]] |
- | [[Category: | + | [[Category: Heme binding]] |
- | [[Category: | + | [[Category: Hemophore]] |
- | [[Category: | + | [[Category: Iron]] |
- | [[Category: | + | [[Category: Iron ligation]] |
- | [[Category: | + | [[Category: Metal-binding]] |
- | [[Category: | + | [[Category: Metal-binding protein]] |
- | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 17:48:34 2008'' | |
- | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + |
Revision as of 14:48, 4 May 2008
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 Sun May 4 17:48:34 2008