2uyd

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|PDB= 2uyd |SIZE=350|CAPTION= <scene name='initialview01'>2uyd</scene>, resolution 2.70&Aring;
|PDB= 2uyd |SIZE=350|CAPTION= <scene name='initialview01'>2uyd</scene>, resolution 2.70&Aring;
|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>
|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>
+
|LIGAND= <scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene>
|ACTIVITY=
|ACTIVITY=
|GENE=
|GENE=
 +
|DOMAIN=
 +
|RELATEDENTRY=[[1b2v|1B2V]], [[1dk0|1DK0]], [[1dkh|1DKH]], [[1ybj|1YBJ]], [[2cn4|2CN4]]
 +
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2uyd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2uyd OCA], [http://www.ebi.ac.uk/pdbsum/2uyd PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2uyd RCSB]</span>
}}
}}
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[[Category: Izadi-Pruneyre, N.]]
[[Category: Izadi-Pruneyre, N.]]
[[Category: Lecroisey, A.]]
[[Category: Lecroisey, A.]]
-
[[Category: ACT]]
 
-
[[Category: HEM]]
 
-
[[Category: ZN]]
 
[[Category: heme]]
[[Category: heme]]
[[Category: heme acquisition system]]
[[Category: heme acquisition system]]
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[[Category: metal-binding protein]]
[[Category: metal-binding protein]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 18:41:16 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 05:06:15 2008''

Revision as of 02:06, 31 March 2008


PDB ID 2uyd

Drag the structure with the mouse to rotate
, resolution 2.70Å
Sites: , , , , , , , , and
Ligands: , ,
Related: 1B2V, 1DK0, 1DKH, 1YBJ, 2CN4


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

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