3uq2: Difference between revisions

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[[Image:3uq2.png|left|200px]]


{{STRUCTURE_3uq2| PDB=3uq2 | SCENE= }}
==Crystal structure of the post-catalytic product complex of polymerase lambda with an rCMP inserted opposite a templating G and dAMP inserted opposite a templating T at the primer terminus.==
<StructureSection load='3uq2' size='340' side='right'caption='[[3uq2]], [[Resolution|resolution]] 2.25&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[3uq2]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3UQ2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3UQ2 FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.25&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=PPV:PYROPHOSPHATE'>PPV</scene></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3uq2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3uq2 OCA], [https://pdbe.org/3uq2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3uq2 RCSB], [https://www.ebi.ac.uk/pdbsum/3uq2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3uq2 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/DPOLL_HUMAN DPOLL_HUMAN] Repair polymerase. Involved in base excision repair (BER) responsible for repair of lesions that give rise to abasic (AP) sites in DNA. Has both DNA polymerase and terminal transferase activities. Has a 5'-deoxyribose-5-phosphate lyase (dRP lyase) activity.<ref>PMID:11457865</ref> <ref>PMID:15537631</ref>


===Crystal structure of the post-catalytic product complex of polymerase lambda with an rAMP inserted opposite a templating G and dAMP inserted opposite a templating T at the primer terminus.===
==See Also==
 
*[[DNA polymerase 3D structures|DNA polymerase 3D structures]]
{{ABSTRACT_PUBMED_22584622}}
== References ==
 
<references/>
==About this Structure==
__TOC__
[[3uq2]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3UQ2 OCA].
</StructureSection>
 
==Reference==
<ref group="xtra">PMID:022584622</ref><references group="xtra"/>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Bebenek, K.]]
[[Category: Large Structures]]
[[Category: Gosavi, R A.]]
[[Category: Bebenek K]]
[[Category: Kunkel, T A.]]
[[Category: Gosavi RA]]
[[Category: Moon, A F.]]
[[Category: Kunkel TA]]
[[Category: Pedersen, L C.]]
[[Category: Moon AF]]
[[Category: Dna polymerase lambda]]
[[Category: Pedersen LC]]
[[Category: Lyase-dna complex]]
[[Category: Protein conformation]]
[[Category: Ribonucleotide incorporation]]
[[Category: Transferase]]

Latest revision as of 17:05, 14 March 2024

Crystal structure of the post-catalytic product complex of polymerase lambda with an rCMP inserted opposite a templating G and dAMP inserted opposite a templating T at the primer terminus.Crystal structure of the post-catalytic product complex of polymerase lambda with an rCMP inserted opposite a templating G and dAMP inserted opposite a templating T at the primer terminus.

Structural highlights

3uq2 is a 4 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.25Å
Ligands:, ,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

DPOLL_HUMAN Repair polymerase. Involved in base excision repair (BER) responsible for repair of lesions that give rise to abasic (AP) sites in DNA. Has both DNA polymerase and terminal transferase activities. Has a 5'-deoxyribose-5-phosphate lyase (dRP lyase) activity.[1] [2]

See Also

References

  1. ↑ Garcia-Diaz M, Bebenek K, Kunkel TA, Blanco L. Identification of an intrinsic 5'-deoxyribose-5-phosphate lyase activity in human DNA polymerase lambda: a possible role in base excision repair. J Biol Chem. 2001 Sep 14;276(37):34659-63. Epub 2001 Jul 16. PMID:11457865 doi:10.1074/jbc.M106336200
  2. ↑ Maga G, Ramadan K, Locatelli GA, Shevelev I, Spadari S, Hubscher U. DNA elongation by the human DNA polymerase lambda polymerase and terminal transferase activities are differentially coordinated by proliferating cell nuclear antigen and replication protein A. J Biol Chem. 2005 Jan 21;280(3):1971-81. Epub 2004 Nov 10. PMID:15537631 doi:10.1074/jbc.M411650200

3uq2, resolution 2.25Å

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