1rzt

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(New page: 200px<br /> <applet load="1rzt" size="450" color="white" frame="true" align="right" spinBox="true" caption="1rzt, resolution 2.10&Aring;" /> '''Crystal structure o...)
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Revision as of 17:02, 12 November 2007


1rzt, resolution 2.10Å

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Crystal structure of DNA polymerase lambda complexed with a two nucleotide gap DNA molecule

Overview

Human DNA polymerase lambda (Pol lambda) is a family X member with low, frameshift fidelity that has been suggested to perform gap-filling DNA, synthesis during base excision repair and during repair of broken ends, with limited homology. Here, we present a 2.1 A crystal structure of the, catalytic core of Pol lambda in complex with DNA containing a two, nucleotide gap. Pol lambda makes limited contacts with the template strand, at the polymerase active site, and superimposition with Pol beta in a, ternary complex suggests a shift in the position of the DNA at the active, site that is reminiscent of a deletion intermediate. Surprisingly, Pol, lambda can adopt a closed conformation, even in the absence of dNTP, binding. These observations have implications for the catalytic mechanism, and putative DNA repair functions of Pol lambda.

About this Structure

1RZT is a Single protein structure of sequence from Homo sapiens with NA and EDO as ligands. Active as DNA-directed DNA polymerase, with EC number 2.7.7.7 Full crystallographic information is available from OCA.

Reference

A structural solution for the DNA polymerase lambda-dependent repair of DNA gaps with minimal homology., Garcia-Diaz M, Bebenek K, Krahn JM, Blanco L, Kunkel TA, Pedersen LC, Mol Cell. 2004 Feb 27;13(4):561-72. PMID:14992725

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