2ig9
From Proteopedia
(New page: 200px<br /><applet load="2ig9" size="350" color="white" frame="true" align="right" spinBox="true" caption="2ig9, resolution 1.90Å" /> '''Structure of a full-...) |
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==Overview== | ==Overview== | ||
| - | We report the structures of three intermediates in the O2 activation and | + | 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== | ==About this Structure== | ||
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[[Category: Brevibacterium fuscum]] | [[Category: Brevibacterium fuscum]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Kovaleva, E | + | [[Category: Kovaleva, E G.]] |
| - | [[Category: Lipscomb, J | + | [[Category: Lipscomb, J D.]] |
[[Category: CA]] | [[Category: CA]] | ||
[[Category: CL]] | [[Category: CL]] | ||
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[[Category: oxygenase]] | [[Category: oxygenase]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:52:20 2008'' |
Revision as of 15:52, 21 February 2008
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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 with , , and as ligands. Active as 3,4-dihydroxyphenylacetate 2,3-dioxygenase, with EC number 1.13.11.15 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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