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New page: left|200px<br /> <applet load="1rzt" size="450" color="white" frame="true" align="right" spinBox="true" caption="1rzt, resolution 2.10Å" /> '''Crystal structure o...
 
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[[Image:1rzt.gif|left|200px]]<br />
[[Image:1rzt.gif|left|200px]]<br /><applet load="1rzt" size="350" color="white" frame="true" align="right" spinBox="true"  
<applet load="1rzt" size="450" color="white" frame="true" align="right" spinBox="true"  
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==
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.
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==
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].  
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.]]
[[Category: Krahn, J.M.]]
[[Category: Krahn, J M.]]
[[Category: Kunkel, T.A.]]
[[Category: Kunkel, T A.]]
[[Category: Pedersen, L.C.]]
[[Category: Pedersen, L C.]]
[[Category: EDO]]
[[Category: EDO]]
[[Category: NA]]
[[Category: NA]]
[[Category: dna polymerase lambda]]
[[Category: dna polymerase lambda]]


''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 19:08:53 2007''
''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

File:1rzt.gif


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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