1fvi
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(New page: 200px<br /> <applet load="1fvi" size="450" color="white" frame="true" align="right" spinBox="true" caption="1fvi, resolution 2.0Å" /> '''CRYSTAL STRUCTURE OF...)
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Revision as of 06:53, 18 November 2007
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CRYSTAL STRUCTURE OF CHLORELLA VIRUS DNA LIGASE-ADENYLATE
Overview
Chlorella virus DNA ligase is the smallest eukaryotic ATP-dependent ligase, known; it has an intrinsic nick-sensing function and suffices for yeast, cell growth. Here, we report the 2.0 A crystal structure of the covalent, ligase-AMP reaction intermediate. The conformation of the adenosine, nucleoside and contacts between the enzyme and the ribose sugar have, undergone a significant change compared to complexes of T7 ligase with ATP, or mRNA capping enzyme with GTP. The conformational switch allows the 3', OH of AMP to coordinate directly the 5' PO(4) of the nick. The structure, explains why nick sensing is restricted to adenylated ligase and why the, 5' phosphate is required for DNA binding. We identify a metal binding site, on ligase-adenylate and propose a mechanism of nick recognition and, catalysis supported by mutational data.
About this Structure
1FVI is a Single protein structure of sequence from Chlorella virus with SO4 and AMP as ligands. The following page contains interesting information on the relation of 1FVI with [DNA Ligase]. Full crystallographic information is available from OCA.
Reference
Crystal structure of eukaryotic DNA ligase-adenylate illuminates the mechanism of nick sensing and strand joining., Odell M, Sriskanda V, Shuman S, Nikolov DB, Mol Cell. 2000 Nov;6(5):1183-93. PMID:11106756
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