2iga: Difference between revisions

Revision as of 18:52, 21 February 2008

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.

OverviewOverview

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 StructureAbout this Structure

2IGA 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.

ReferenceReference

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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 ==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.
+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==
@@ Line 14: / Line 14: @@
 [[Category: Brevibacterium fuscum]]
 [[Category: Single protein]]
-[[Category: Kovaleva, E.G.]]
+[[Category: Kovaleva, E G.]]
-[[Category: Lipscomb, J.D.]]
+[[Category: Lipscomb, J D.]]
 [[Category: CA]]
 [[Category: CL]]
@@ Line 32: / Line 32: @@
 [[Category: substrate-semiquinone]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jan 23 14:47:27 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:52:19 2008''