1xsn: Difference between revisions

From Proteopedia
Jump to navigation Jump to search
No edit summary
No edit summary
 
(8 intermediate revisions by the same user not shown)
Line 1: Line 1:
[[Image:1xsn.png|left|200px]]


{{STRUCTURE_1xsn|  PDB=1xsn  |  SCENE=  }}
==Crystal Structure of human DNA polymerase lambda in complex with a one nucleotide DNA gap and ddTTP==
 
<StructureSection load='1xsn' size='340' side='right'caption='[[1xsn]], [[Resolution|resolution]] 1.95&Aring;' scene=''>
===Crystal Structure of human DNA polymerase lambda in complex with a one nucleotide DNA gap and ddTTP===
== Structural highlights ==
 
<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>
{{ABSTRACT_PUBMED_15608652}}
</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>
 
<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>
==About this Structure==
<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>
[[1xsn]] is a 4 chain structure of [[DNA polymerase]] 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=1XSN OCA].  
</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>


==See Also==
==See Also==
*[[DNA polymerase|DNA polymerase]]
*[[DNA polymerase 3D structures|DNA polymerase 3D structures]]
 
== References ==
==Reference==
<references/>
<ref group="xtra">PMID:015608652</ref><references group="xtra"/>
__TOC__
[[Category: DNA-directed DNA polymerase]]
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Bebenek, K.]]
[[Category: Large Structures]]
[[Category: Garcia-Diaz, M.]]
[[Category: Bebenek K]]
[[Category: Krahn, J M.]]
[[Category: Garcia-Diaz M]]
[[Category: Kunkel, T A.]]
[[Category: Krahn JM]]
[[Category: Pedersen, L C.]]
[[Category: Kunkel TA]]
[[Category: Dna polymerase lambda]]
[[Category: Pedersen LC]]
[[Category: Helix-hairpin-helix]]
[[Category: Protein-dna complex]]
[[Category: Transferase-dna complex]]

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

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA