1oao

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|PDB= 1oao |SIZE=350|CAPTION= <scene name='initialview01'>1oao</scene>, resolution 1.90&Aring;
|PDB= 1oao |SIZE=350|CAPTION= <scene name='initialview01'>1oao</scene>, resolution 1.90&Aring;
|SITE= <scene name='pdbsite=AC1:So4+Binding+Site+For+Chain+D'>AC1</scene>
|SITE= <scene name='pdbsite=AC1:So4+Binding+Site+For+Chain+D'>AC1</scene>
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|LIGAND= <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=FE2:FE+(II)+ION'>FE2</scene>, <scene name='pdbligand=BCT:BICARBONATE+ION'>BCT</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene>, <scene name='pdbligand=NI:NICKEL+(II)+ION'>NI</scene>, <scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=SF4:IRON/SULFUR+CLUSTER'>SF4</scene>, <scene name='pdbligand=XCC:FE(4)-NI(1)-S(4)+CLUSTER'>XCC</scene>, <scene name='pdbligand=SX:SULFUR+OXIDE'>SX</scene>, <scene name='pdbligand=FLH:FORMALDEHYDE'>FLH</scene> and <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>
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|LIGAND= <scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=BCT:BICARBONATE+ION'>BCT</scene>, <scene name='pdbligand=FE2:FE+(II)+ION'>FE2</scene>, <scene name='pdbligand=FLH:FORMALDEHYDE'>FLH</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NI:NICKEL+(II)+ION'>NI</scene>, <scene name='pdbligand=SF4:IRON/SULFUR+CLUSTER'>SF4</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=SX:SULFUR+OXIDE'>SX</scene>, <scene name='pdbligand=XCC:FE(4)-NI(1)-S(4)+CLUSTER'>XCC</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene>
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|ACTIVITY= [http://en.wikipedia.org/wiki/Carbon-monoxide_dehydrogenase_(acceptor) Carbon-monoxide dehydrogenase (acceptor)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.2.99.2 1.2.99.2]
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|ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Carbon-monoxide_dehydrogenase_(acceptor) Carbon-monoxide dehydrogenase (acceptor)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.2.99.2 1.2.99.2] </span>
|GENE=
|GENE=
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|DOMAIN=
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|RELATEDENTRY=
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1oao FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1oao OCA], [http://www.ebi.ac.uk/pdbsum/1oao PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1oao RCSB]</span>
}}
}}
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[[Category: Vernede, X.]]
[[Category: Vernede, X.]]
[[Category: Volbeda, A.]]
[[Category: Volbeda, A.]]
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[[Category: ACT]]
 
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[[Category: BCT]]
 
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[[Category: FE2]]
 
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[[Category: FLH]]
 
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[[Category: GOL]]
 
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[[Category: NI]]
 
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[[Category: SF4]]
 
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[[Category: SO4]]
 
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[[Category: SX]]
 
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[[Category: XCC]]
 
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[[Category: ZN]]
 
[[Category: acetyl-coa formation]]
[[Category: acetyl-coa formation]]
[[Category: electron transfer]]
[[Category: electron transfer]]
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[[Category: nickel]]
 
[[Category: oxidoreductase]]
[[Category: oxidoreductase]]
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[[Category: wood/ljungdahl pathway]]
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[[Category: wood/ljungdahl pathway,nickel]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 13:08:13 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:42:30 2008''

Revision as of 19:42, 30 March 2008


PDB ID 1oao

Drag the structure with the mouse to rotate
, resolution 1.90Å
Sites:
Ligands: , , , , , , , , , ,
Activity: Carbon-monoxide dehydrogenase (acceptor), with EC number 1.2.99.2
Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



NIZN[FE4S4] AND NINI[FE4S4] CLUSTERS IN CLOSED AND OPEN ALPHA SUBUNITS OF ACETYL-COA SYNTHASE/CARBON MONOXIDE DEHYDROGENASE


Overview

The crystal structure of the tetrameric alpha2beta2 acetyl-coenzyme A synthase/carbon monoxide dehydrogenase from Moorella thermoacetica has been solved at 1.9 A resolution. Surprisingly, the two alpha subunits display different (open and closed) conformations. Furthermore, X-ray data collected from crystals near the absorption edges of several metal ions indicate that the closed form contains one Zn and one Ni at its active site metal cluster (A-cluster) in the alpha subunit, whereas the open form has two Ni ions at the corresponding positions. Alternative metal contents at the active site have been observed in a recent structure of the same protein in which A-clusters contained one Cu and one Ni, and in reconstitution studies of a recombinant apo form of a related acetyl-CoA synthase. On the basis of our observations along with previously reported data, we postulate that only the A-clusters containing two Ni ions are catalytically active.

About this Structure

1OAO is a Protein complex structure of sequences from Moorella thermoacetica. Full crystallographic information is available from OCA.

Reference

Ni-Zn-[Fe4-S4] and Ni-Ni-[Fe4-S4] clusters in closed and open subunits of acetyl-CoA synthase/carbon monoxide dehydrogenase., Darnault C, Volbeda A, Kim EJ, Legrand P, Vernede X, Lindahl PA, Fontecilla-Camps JC, Nat Struct Biol. 2003 Apr;10(4):271-9. PMID:12627225

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