2uyd
From Proteopedia
(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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==Overview== | ==Overview== | ||
| - | Heme carrier HasA has a unique type of histidine/tyrosine heme iron | + | 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== | ==About this Structure== | ||
| - | 2UYD is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Serratia_marcescens Serratia marcescens] with <scene name='pdbligand=ZN:'>ZN</scene>, <scene name='pdbligand=ACT:'>ACT</scene> and <scene name='pdbligand=HEM:'>HEM</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Known structural/functional Sites: <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>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2UYD OCA]. | + | 2UYD is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Serratia_marcescens Serratia marcescens] with <scene name='pdbligand=ZN:'>ZN</scene>, <scene name='pdbligand=ACT:'>ACT</scene> and <scene name='pdbligand=HEM:'>HEM</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Known structural/functional Sites: <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>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2UYD OCA]. |
==Reference== | ==Reference== | ||
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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 Feb 21 18:51:36 2008'' |
Revision as of 16:51, 21 February 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
Page seeded by OCA on Thu Feb 21 18:51:36 2008
