This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
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...) |
|||
| Line 4: | Line 4: | ||
==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== | ||
| Line 31: | Line 31: | ||
[[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
|
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
