1xdq: Difference between revisions

Revision as of 08:27, 29 July 2008

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File:1xdq.png

Template:STRUCTURE 1xdq

Structural and Biochemical Identification of a Novel Bacterial OxidoreductaseStructural and Biochemical Identification of a Novel Bacterial Oxidoreductase

Template:ABSTRACT PUBMED 15355966

About this StructureAbout this Structure

1XDQ is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.

ReferenceReference

Structural and biochemical identification of a novel bacterial oxidoreductase., Loschi L, Brokx SJ, Hills TL, Zhang G, Bertero MG, Lovering AL, Weiner JH, Strynadka NC, J Biol Chem. 2004 Nov 26;279(48):50391-400. Epub 2004 Sep 7. PMID:15355966

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OCA

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-'''Structural and Biochemical Identification of a Novel Bacterial Oxidoreductase'''
+===Structural and Biochemical Identification of a Novel Bacterial Oxidoreductase===
-==Overview==
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-By using a bioinformatics screen of the Escherichia coli genome for potential molybdenum-containing enzymes, we have identified a novel oxidoreductase conserved in the majority of Gram-negative bacteria. The identified operon encodes for a proposed heterodimer, YedYZ in Escherichia coli, consisting of a soluble catalytic subunit termed YedY, which is likely anchored to the membrane by a heme-containing trans-membrane subunit termed YedZ. YedY is uniquely characterized by the presence of one molybdenum molybdopterin not conjugated by an additional nucleotide, and it represents the only molybdoenzyme isolated from E. coli characterized by the presence of this cofactor form. We have further characterized the catalytic subunit YedY in both the molybdenum- and tungsten-substituted forms by using crystallographic analysis. YedY is very distinct in overall architecture from all known bacterial reductases but does show some similarity with the catalytic domain of the eukaryotic chicken liver sulfite oxidase. However, the strictly conserved residues involved in the metal coordination sphere and in the substrate binding pocket of YedY are strikingly different from that of chicken liver sulfite oxidase, suggesting a catalytic activity more in keeping with a reductase than that of a sulfite oxidase. Preliminary kinetic analysis of YedY with a variety of substrates supports our proposal that YedY and its many orthologues may represent a new type of membrane-associated bacterial reductase.
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+{{ABSTRACT_PUBMED_15355966}}
 ==About this Structure==
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 [[Category: Oxidoreductase]]
 [[Category: Sequence analysis]]
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