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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[[Image:1rzt.gif|left|200px]]<br /><applet load="1rzt" size="350" color="white" frame="true" align="right" spinBox="true"
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<applet load="1rzt" size="450" color="white" frame="true" align="right" spinBox="true"
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caption="1rzt, resolution 2.10&Aring;" />
caption="1rzt, resolution 2.10&Aring;" />
'''Crystal structure of DNA polymerase lambda complexed with a two nucleotide gap DNA molecule'''<br />
'''Crystal structure of DNA polymerase lambda complexed with a two nucleotide gap DNA molecule'''<br />
==Overview==
==Overview==
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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.
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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==
==About this Structure==
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1RZT is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with NA and EDO as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/DNA-directed_DNA_polymerase DNA-directed DNA polymerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.7.7 2.7.7.7] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1RZT OCA].
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1RZT is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=NA:'>NA</scene> and <scene name='pdbligand=EDO:'>EDO</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/DNA-directed_DNA_polymerase DNA-directed DNA polymerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.7.7 2.7.7.7] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1RZT OCA].
==Reference==
==Reference==
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[[Category: Blanco, L.]]
[[Category: Blanco, L.]]
[[Category: Garcia-Diaz, M.]]
[[Category: Garcia-Diaz, M.]]
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[[Category: Krahn, J.M.]]
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[[Category: Krahn, J M.]]
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[[Category: Kunkel, T.A.]]
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[[Category: Kunkel, T A.]]
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[[Category: Pedersen, L.C.]]
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[[Category: Pedersen, L C.]]
[[Category: EDO]]
[[Category: EDO]]
[[Category: NA]]
[[Category: NA]]
[[Category: dna polymerase lambda]]
[[Category: dna polymerase lambda]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 19:08:53 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:56:21 2008''

Revision as of 12:56, 21 February 2008


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 and 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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