2uyd
From Proteopedia
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- | [[Image:2uyd.jpg|left|200px]] | + | [[Image:2uyd.jpg|left|200px]] |
- | + | ||
- | '''CRYSTAL STRUCTURE OF THE SMHASA MUTANT H83A''' | + | {{Structure |
+ | |PDB= 2uyd |SIZE=350|CAPTION= <scene name='initialview01'>2uyd</scene>, resolution 2.70Å | ||
+ | |SITE= <scene name='pdbsite=AC1:Hem+Binding+Site+For+Chain+X'>AC1</scene>, <scene name='pdbsite=AC2:Zn+Binding+Site+For+Chain+X'>AC2</scene>, <scene name='pdbsite=AC3:Zn+Binding+Site+For+Chain+X'>AC3</scene>, <scene name='pdbsite=AC4:Zn+Binding+Site+For+Chain+X'>AC4</scene>, <scene name='pdbsite=AC5:Zn+Binding+Site+For+Chain+X'>AC5</scene>, <scene name='pdbsite=AC7:Zn+Binding+Site+For+Chain+X'>AC7</scene>, <scene name='pdbsite=AC8:Zn+Binding+Site+For+Chain+X'>AC8</scene>, <scene name='pdbsite=AC9:Zn+Binding+Site+For+Chain+X'>AC9</scene>, <scene name='pdbsite=BC1:Act+Binding+Site+For+Chain+X'>BC1</scene> and <scene name='pdbsite=BC2:Act+Binding+Site+For+Chain+X'>BC2</scene> | ||
+ | |LIGAND= <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene>, <scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene> and <scene name='pdbligand=HEM:PROTOPORPHYRIN IX CONTAINING FE'>HEM</scene> | ||
+ | |ACTIVITY= | ||
+ | |GENE= | ||
+ | }} | ||
+ | |||
+ | '''CRYSTAL STRUCTURE OF THE SMHASA MUTANT H83A''' | ||
+ | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
- | 2UYD is a [ | + | 2UYD is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Serratia_marcescens Serratia marcescens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2UYD OCA]. |
==Reference== | ==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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/18162469 18162469] |
[[Category: Serratia marcescens]] | [[Category: Serratia marcescens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: metal-binding protein]] | [[Category: metal-binding protein]] | ||
- | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 18:41:16 2008'' |
Revision as of 16:41, 20 March 2008
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, resolution 2.70Å | |||||||
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Sites: | , , , , , , , , and | ||||||
Ligands: | , and | ||||||
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
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