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2iga

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|PDB= 2iga |SIZE=350|CAPTION= <scene name='initialview01'>2iga</scene>, resolution 1.95&Aring;
|PDB= 2iga |SIZE=350|CAPTION= <scene name='initialview01'>2iga</scene>, resolution 1.95&Aring;
|SITE=
|SITE=
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|LIGAND= <scene name='pdbligand=FE2:FE+(II)+ION'>FE2</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=XXP:2-KETO,5-NITRO,6-HYDROXY-3,5-HEXADIENOIC+ACID'>XXP</scene>, <scene name='pdbligand=XX3:(1S)-1-HYDROPEROXY-1-HYDROXY-2-KETO-5-NITROCYCLOHEXA-3,5-DIENE'>XX3</scene>, <scene name='pdbligand=XX2:1-KETO,2-HYDROXY,4-NITROBENZENE,+1+ELECTRON+OXIDIZED'>XX2</scene>, <scene name='pdbligand=OXY:OXYGEN+MOLECULE'>OXY</scene> and <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>
+
|LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=FE2:FE+(II)+ION'>FE2</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=OXY:OXYGEN+MOLECULE'>OXY</scene>, <scene name='pdbligand=XX2:1-KETO,2-HYDROXY,4-NITROBENZENE,+1+ELECTRON+OXIDIZED'>XX2</scene>, <scene name='pdbligand=XX3:(1S)-1-HYDROPEROXY-1-HYDROXY-2-KETO-5-NITROCYCLOHEXA-3,5-DIENE'>XX3</scene>, <scene name='pdbligand=XXP:2-KETO,5-NITRO,6-HYDROXY-3,5-HEXADIENOIC+ACID'>XXP</scene>
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|ACTIVITY= [http://en.wikipedia.org/wiki/3,4-dihydroxyphenylacetate_2,3-dioxygenase 3,4-dihydroxyphenylacetate 2,3-dioxygenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.13.11.15 1.13.11.15]
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|ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/3,4-dihydroxyphenylacetate_2,3-dioxygenase 3,4-dihydroxyphenylacetate 2,3-dioxygenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.13.11.15 1.13.11.15] </span>
|GENE= hpcd ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=47914 Brevibacterium fuscum])
|GENE= hpcd ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=47914 Brevibacterium fuscum])
 +
|DOMAIN=
 +
|RELATEDENTRY=[[2ig9|2IG9]]
 +
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2iga FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2iga OCA], [http://www.ebi.ac.uk/pdbsum/2iga PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2iga RCSB]</span>
}}
}}
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[[Category: Kovaleva, E G.]]
[[Category: Kovaleva, E G.]]
[[Category: Lipscomb, J D.]]
[[Category: Lipscomb, J D.]]
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[[Category: CA]]
 
-
[[Category: CL]]
 
-
[[Category: FE2]]
 
-
[[Category: GOL]]
 
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[[Category: OXY]]
 
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[[Category: XX2]]
 
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[[Category: XX3]]
 
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[[Category: XXP]]
 
[[Category: alkylperoxo intermediate]]
[[Category: alkylperoxo intermediate]]
[[Category: extradiol]]
[[Category: extradiol]]
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[[Category: substrate-semiquinone]]
[[Category: substrate-semiquinone]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 17:29:09 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 03:43:53 2008''

Revision as of 00:43, 31 March 2008


PDB ID 2iga

Drag the structure with the mouse to rotate
, resolution 1.95Å
Ligands: , , , , , , ,
Gene: hpcd (Brevibacterium fuscum)
Activity: 3,4-dihydroxyphenylacetate 2,3-dioxygenase, with EC number 1.13.11.15
Related: 2IG9


Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



Structure of Homoprotocatechuate 2,3-Dioxygenase from B. fuscum in complex with reactive intermediates formed via in crystallo reaction with 4-nitrocatechol at low oxygen concentrations.


Overview

We report the structures of three intermediates in the O2 activation and insertion reactions of an extradiol ring-cleaving dioxygenase. A crystal of Fe2+-containing homoprotocatechuate 2,3-dioxygenase was soaked in the slow substrate 4-nitrocatechol in a low O2 atmosphere. The x-ray crystal structure shows that three different intermediates reside in different subunits of a single homotetrameric enzyme molecule. One of these is the key substrate-alkylperoxo-Fe2+ intermediate, which has been predicted, but not structurally characterized, in an oxygenase. The intermediates define the major chemical steps of the dioxygenase mechanism and point to a general mechanistic strategy for the diverse 2-His-1-carboxylate enzyme family.

About this Structure

2IGA is a Single protein structure of sequence from Brevibacterium fuscum. Full crystallographic information is available from OCA.

Reference

Crystal structures of Fe2+ dioxygenase superoxo, alkylperoxo, and bound product intermediates., Kovaleva EG, Lipscomb JD, Science. 2007 Apr 20;316(5823):453-7. PMID:17446402

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