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2ig9
From Proteopedia
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[[Image:2ig9.gif|left|200px]] | [[Image:2ig9.gif|left|200px]] | ||
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'''Structure of a full-length Homoprotocatechuate 2,3-Dioxygenase from B. fuscum in a new spacegroup.''' | '''Structure of a full-length Homoprotocatechuate 2,3-Dioxygenase from B. fuscum in a new spacegroup.''' | ||
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[[Category: Kovaleva, E G.]] | [[Category: Kovaleva, E G.]] | ||
[[Category: Lipscomb, J D.]] | [[Category: Lipscomb, J D.]] | ||
| - | [[Category: | + | [[Category: Extradiol]] |
| - | [[Category: | + | [[Category: Homoprotocatechuate]] |
| - | [[Category: | + | [[Category: Oxygenase]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 07:28:02 2008'' | |
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| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 04:28, 4 May 2008
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 Sun May 4 07:28:02 2008
