1hu0 | pdb_00001hu0

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Revision as of 15:16, 12 November 2007 by OCA (talk | contribs) (New page: left|200px<br /> <applet load="1hu0" size="450" color="white" frame="true" align="right" spinBox="true" caption="1hu0, resolution 2.35Å" /> '''CRYSTAL STRUCTURE O...)
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CRYSTAL STRUCTURE OF AN HOGG1-DNA BOROHYDRIDE TRAPPED INTERMEDIATE COMPLEX

File:1hu0.gif


1hu0, resolution 2.35Å

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Overview

Most spontaneous damage to bases in DNA is corrected through the action of, the base-excision DNA repair pathway. Base excision repair is initiated by, DNA glycosylases, lesion-specific enzymes that intercept aberrant bases in, DNA and catalyze their excision. How such proteins accomplish the feat of, catalyzing no fewer than five sequential reaction steps using a single, active site has been unknown. To help answer this, we report the structure, of a trapped catalytic intermediate in DNA repair by human 8-oxoguanine, DNA glycosylase. This structure and supporting biochemical results reveal, that the enzyme sequesters the excised lesion base and exploits it as a, cofactor to participate in catalysis. To our knowledge, the present, example represents the first documented case of product-assisted catalysis, in an enzyme-catalyzed reaction.

Disease

Known disease associated with this structure: Renal cell carcinoma, clear cell, somatic OMIM:[601982]

About this Structure

1HU0 is a Single protein structure of sequence from Homo sapiens with CA and OXG as ligands. Full crystallographic information is available from OCA.

Reference

Product-assisted catalysis in base-excision DNA repair., Fromme JC, Bruner SD, Yang W, Karplus M, Verdine GL, Nat Struct Biol. 2003 Mar;10(3):204-11. PMID:12592398

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