2iga

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[[Image:2iga.gif|left|200px]]<br /><applet load="2iga" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:2iga.gif|left|200px]]
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caption="2iga, resolution 1.95&Aring;" />
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'''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.'''<br />
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{{Structure
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|PDB= 2iga |SIZE=350|CAPTION= <scene name='initialview01'>2iga</scene>, resolution 1.95&Aring;
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|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>
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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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|GENE= hpcd ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=47914 Brevibacterium fuscum])
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}}
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'''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.'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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2IGA is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Brevibacterium_fuscum Brevibacterium fuscum] with <scene name='pdbligand=FE2:'>FE2</scene>, <scene name='pdbligand=CL:'>CL</scene>, <scene name='pdbligand=CA:'>CA</scene>, <scene name='pdbligand=XXP:'>XXP</scene>, <scene name='pdbligand=XX3:'>XX3</scene>, <scene name='pdbligand=XX2:'>XX2</scene>, <scene name='pdbligand=OXY:'>OXY</scene> and <scene name='pdbligand=GOL:'>GOL</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [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] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2IGA OCA].
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2IGA is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Brevibacterium_fuscum Brevibacterium fuscum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2IGA OCA].
==Reference==
==Reference==
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Crystal structures of Fe2+ dioxygenase superoxo, alkylperoxo, and bound product intermediates., Kovaleva EG, Lipscomb JD, Science. 2007 Apr 20;316(5823):453-7. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17446402 17446402]
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Crystal structures of Fe2+ dioxygenase superoxo, alkylperoxo, and bound product intermediates., Kovaleva EG, Lipscomb JD, Science. 2007 Apr 20;316(5823):453-7. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17446402 17446402]
[[Category: 3,4-dihydroxyphenylacetate 2,3-dioxygenase]]
[[Category: 3,4-dihydroxyphenylacetate 2,3-dioxygenase]]
[[Category: Brevibacterium fuscum]]
[[Category: Brevibacterium fuscum]]
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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 Feb 21 17:52:19 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 17:29:09 2008''

Revision as of 15:29, 20 March 2008

Image:2iga.gif


PDB ID 2iga

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