2gws
From Proteopedia
(New page: 200px<br /> <applet load="2gws" size="450" color="white" frame="true" align="right" spinBox="true" caption="2gws, resolution 2.400Å" /> '''Crystal Structure ...) |
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| - | [[Image:2gws.gif|left|200px]]<br /> | + | [[Image:2gws.gif|left|200px]]<br /><applet load="2gws" size="350" color="white" frame="true" align="right" spinBox="true" |
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caption="2gws, resolution 2.400Å" /> | caption="2gws, resolution 2.400Å" /> | ||
'''Crystal Structure of human DNA Polymerase lambda with a G/G mismatch in the primer terminus'''<br /> | '''Crystal Structure of human DNA Polymerase lambda with a G/G mismatch in the primer terminus'''<br /> | ||
==Overview== | ==Overview== | ||
| - | DNA polymerase lambda (Pol lambda) is one of several DNA polymerases | + | DNA polymerase lambda (Pol lambda) is one of several DNA polymerases suggested to participate in base excision repair (BER), in repair of broken DNA ends and in translesion synthesis. It has been proposed that the nature of the DNA intermediates partly determines which polymerase is used for a particular repair reaction. To test this hypothesis, here we examine the ability of human Pol lambda to extend mismatched primer-termini, either on 'open' template-primer substrates, or on its preferred substrate, a 1 nt gapped-DNA molecule having a 5'-phosphate. Interestingly, Pol lambda extended mismatches with an average efficiency of approximately 10(-2) relative to matched base pairs. The match and mismatch extension catalytic efficiencies obtained on gapped molecules were approximately 260-fold higher than on template-primer molecules. A crystal structure of Pol lambda in complex with a single-nucleotide gap containing a dG.dGMP mismatch at the primer-terminus (2.40 A) suggests that, at least for certain mispairs, Pol lambda is unable to differentiate between matched and mismatched termini during the DNA binding step, thus accounting for the relatively high efficiency of mismatch extension. This property of Pol lambda suggests a potential role as a 'mismatch extender' during non-homologous end joining (NHEJ), and possibly during translesion synthesis. |
==About this Structure== | ==About this Structure== | ||
| - | 2GWS 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, MG, CAC, CL and EDO as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | + | 2GWS 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>, <scene name='pdbligand=MG:'>MG</scene>, <scene name='pdbligand=CAC:'>CAC</scene>, <scene name='pdbligand=CL:'>CL</scene> and <scene name='pdbligand=EDO:'>EDO</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2GWS OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Blanco, L.]] | [[Category: Blanco, L.]] | ||
[[Category: Garcia-Diaz, M.]] | [[Category: Garcia-Diaz, M.]] | ||
| - | [[Category: Kunkel, T | + | [[Category: Kunkel, T A.]] |
| - | [[Category: Pedersen, L | + | [[Category: Pedersen, L C.]] |
| - | [[Category: Picher, A | + | [[Category: Picher, A J.]] |
[[Category: CAC]] | [[Category: CAC]] | ||
[[Category: CL]] | [[Category: CL]] | ||
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[[Category: nhej]] | [[Category: nhej]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:36:10 2008'' |
Revision as of 15:36, 21 February 2008
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Crystal Structure of human DNA Polymerase lambda with a G/G mismatch in the primer terminus
Overview
DNA polymerase lambda (Pol lambda) is one of several DNA polymerases suggested to participate in base excision repair (BER), in repair of broken DNA ends and in translesion synthesis. It has been proposed that the nature of the DNA intermediates partly determines which polymerase is used for a particular repair reaction. To test this hypothesis, here we examine the ability of human Pol lambda to extend mismatched primer-termini, either on 'open' template-primer substrates, or on its preferred substrate, a 1 nt gapped-DNA molecule having a 5'-phosphate. Interestingly, Pol lambda extended mismatches with an average efficiency of approximately 10(-2) relative to matched base pairs. The match and mismatch extension catalytic efficiencies obtained on gapped molecules were approximately 260-fold higher than on template-primer molecules. A crystal structure of Pol lambda in complex with a single-nucleotide gap containing a dG.dGMP mismatch at the primer-terminus (2.40 A) suggests that, at least for certain mispairs, Pol lambda is unable to differentiate between matched and mismatched termini during the DNA binding step, thus accounting for the relatively high efficiency of mismatch extension. This property of Pol lambda suggests a potential role as a 'mismatch extender' during non-homologous end joining (NHEJ), and possibly during translesion synthesis.
About this Structure
2GWS is a Single protein structure of sequence from Homo sapiens with , , , and as ligands. Full crystallographic information is available from OCA.
Reference
Promiscuous mismatch extension by human DNA polymerase lambda., Picher AJ, Garcia-Diaz M, Bebenek K, Pedersen LC, Kunkel TA, Blanco L, Nucleic Acids Res. 2006 Jun 28;34(11):3259-66. Print 2006. PMID:16807316
Page seeded by OCA on Thu Feb 21 17:36:10 2008
Categories: Homo sapiens | Single protein | Bebenek, K. | Blanco, L. | Garcia-Diaz, M. | Kunkel, T A. | Pedersen, L C. | Picher, A J. | CAC | CL | EDO | MG | NA | Crystal structure | Dna polymerase lambda | Family x | Mismatch extension | Mutagenesis | Nhej
