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2ig9
From Proteopedia
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| - | [[Image:2ig9.gif|left|200px]] | + | [[Image:2ig9.gif|left|200px]] |
| - | + | ||
| - | '''Structure of a full-length Homoprotocatechuate 2,3-Dioxygenase from B. fuscum in a new spacegroup.''' | + | {{Structure |
| + | |PDB= 2ig9 |SIZE=350|CAPTION= <scene name='initialview01'>2ig9</scene>, resolution 1.90Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=FE2:FE+(II)+ION'>FE2</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene> and <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene> | ||
| + | |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] | ||
| + | |GENE= hpcd ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=47914 Brevibacterium fuscum]) | ||
| + | }} | ||
| + | |||
| + | '''Structure of a full-length Homoprotocatechuate 2,3-Dioxygenase from B. fuscum in a new spacegroup.''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 2IG9 is a [ | + | 2IG9 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=2IG9 OCA]. |
==Reference== | ==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:[http:// | + | 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: oxygenase]] | [[Category: oxygenase]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 17:29:11 2008'' |
Revision as of 15:29, 20 March 2008
| |||||||
| , resolution 1.90Å | |||||||
|---|---|---|---|---|---|---|---|
| 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 a full-length Homoprotocatechuate 2,3-Dioxygenase from B. fuscum in a new spacegroup.
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
2IG9 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
Page seeded by OCA on Thu Mar 20 17:29:11 2008
