1rzt
From Proteopedia
(Difference between revisions)
| Line 3: | Line 3: | ||
<StructureSection load='1rzt' size='340' side='right'caption='[[1rzt]], [[Resolution|resolution]] 2.10Å' scene=''> | <StructureSection load='1rzt' size='340' side='right'caption='[[1rzt]], [[Resolution|resolution]] 2.10Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[1rzt]] is a 16 chain structure with sequence from [ | + | <table><tr><td colspan='2'>[[1rzt]] is a 16 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=1RZT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1RZT FirstGlance]. <br> |
| - | </td></tr><tr id=' | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.1Å</td></tr> |
| - | <tr id=' | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</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=1rzt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1rzt OCA], [https://pdbe.org/1rzt PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1rzt RCSB], [https://www.ebi.ac.uk/pdbsum/1rzt PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1rzt ProSAT]</span></td></tr> | |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | |
</table> | </table> | ||
== Function == | == 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> |
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
| Line 21: | Line 20: | ||
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1rzt ConSurf]. | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1rzt ConSurf]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
| - | <div style="background-color:#fffaf0;"> | ||
| - | == Publication Abstract from PubMed == | ||
| - | 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. | ||
| - | |||
| - | 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<ref>PMID:14992725</ref> | ||
| - | |||
| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| - | </div> | ||
| - | <div class="pdbe-citations 1rzt" style="background-color:#fffaf0;"></div> | ||
==See Also== | ==See Also== | ||
| Line 37: | Line 27: | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| - | [[Category: | + | [[Category: Homo sapiens]] |
| - | + | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| - | [[Category: Bebenek | + | [[Category: Bebenek K]] |
| - | [[Category: Blanco | + | [[Category: Blanco L]] |
| - | [[Category: Garcia-Diaz | + | [[Category: Garcia-Diaz M]] |
| - | [[Category: Krahn | + | [[Category: Krahn JM]] |
| - | [[Category: Kunkel | + | [[Category: Kunkel TA]] |
| - | [[Category: Pedersen | + | [[Category: Pedersen LC]] |
| - | + | ||
| - | + | ||
Revision as of 06:13, 3 April 2024
Crystal structure of DNA polymerase lambda complexed with a two nucleotide gap DNA molecule
| |||||||||||
