1xsn: Difference between revisions

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{{Seed}}
[[Image:1xsn.png|left|200px]]


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==Crystal Structure of human DNA polymerase lambda in complex with a one nucleotide DNA gap and ddTTP==
The line below this paragraph, containing "STRUCTURE_1xsn", creates the "Structure Box" on the page.
<StructureSection load='1xsn' size='340' side='right'caption='[[1xsn]], [[Resolution|resolution]] 1.95&Aring;' scene=''>
You may change the PDB parameter (which sets the PDB file loaded into the applet)  
== Structural highlights ==
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
<table><tr><td colspan='2'>[[1xsn]] 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=1XSN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1XSN FirstGlance]. <br>
or leave the SCENE parameter empty for the default display.
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.95&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=2DT:3-DEOXYTHYMIDINE-5-MONOPHOSPHATE'>2DT</scene>, <scene name='pdbligand=D3T:2,3-DIDEOXY-THYMIDINE-5-TRIPHOSPHATE'>D3T</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr>
{{STRUCTURE_1xsn| PDB=1xsn |  SCENE= }}
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1xsn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1xsn OCA], [https://pdbe.org/1xsn PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1xsn RCSB], [https://www.ebi.ac.uk/pdbsum/1xsn PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1xsn 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>
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/xs/1xsn_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</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=1xsn ConSurf].
<div style="clear:both"></div>


===Crystal Structure of human DNA polymerase lambda in complex with a one nucleotide DNA gap and ddTTP===
==See Also==
 
*[[DNA polymerase 3D structures|DNA polymerase 3D structures]]
 
== References ==
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{{ABSTRACT_PUBMED_15608652}}
 
==About this Structure==
1XSN is a [[Single protein]] structure of 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=1XSN OCA].
 
==Reference==
A closed conformation for the Pol lambda catalytic cycle., Garcia-Diaz M, Bebenek K, Krahn JM, Kunkel TA, Pedersen LC, Nat Struct Mol Biol. 2005 Jan;12(1):97-8. Epub 2004 Dec 19. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15608652 15608652]
[[Category: DNA-directed DNA polymerase]]
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Bebenek, K.]]
[[Category: Bebenek K]]
[[Category: Garcia-Diaz, M.]]
[[Category: Garcia-Diaz M]]
[[Category: Krahn, J M.]]
[[Category: Krahn JM]]
[[Category: Kunkel, T A.]]
[[Category: Kunkel TA]]
[[Category: Pedersen, L C.]]
[[Category: Pedersen LC]]
[[Category: Dna polymerase lambda]]
[[Category: Helix-hairpin-helix]]
[[Category: Protein-dna complex]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 09:34:18 2008''

Latest revision as of 11:53, 14 February 2024

Crystal Structure of human DNA polymerase lambda in complex with a one nucleotide DNA gap and ddTTPCrystal Structure of human DNA polymerase lambda in complex with a one nucleotide DNA gap and ddTTP

Structural highlights

1xsn 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 1.95Å
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]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

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

1xsn, resolution 1.95Å

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