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2ig9

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Image:2ig9.gif

2ig9, resolution 1.90Å

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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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