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New page: left|200px<br /> <applet load="1xsl" size="450" color="white" frame="true" align="right" spinBox="true" caption="1xsl, resolution 2.30Å" /> '''Crystal Structure o...
 
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'''Crystal Structure of human DNA polymerase lambda in complex with a one nucleotide DNA gap'''<br />


==Overview==
==Crystal Structure of human DNA polymerase lambda in complex with a one nucleotide DNA gap==
Pol lambda is a family X member believed to fill short gaps during DNA, repair. Here we report crystal structures of Pol lambda representing three, steps in filling a single-nucleotide gap. These structures indicate that, unlike other DNA polymerases, Pol lambda does not undergo large subdomain, movements during catalysis, and they provide a clear characterization of, the geometry and stereochemistry of the in-line nucleotidyl transfer, reaction.
<StructureSection load='1xsl' size='340' side='right'caption='[[1xsl]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1xsl]] 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=1XSL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1XSL 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]] 2.3&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CAC:CACODYLATE+ION'>CAC</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</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=1xsl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1xsl OCA], [https://pdbe.org/1xsl PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1xsl RCSB], [https://www.ebi.ac.uk/pdbsum/1xsl PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1xsl ProSAT]</span></td></tr>
</table>
== 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/1xsl_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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=1xsl ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Pol lambda is a family X member believed to fill short gaps during DNA repair. Here we report crystal structures of Pol lambda representing three steps in filling a single-nucleotide gap. These structures indicate that, unlike other DNA polymerases, Pol lambda does not undergo large subdomain movements during catalysis, and they provide a clear characterization of the geometry and stereochemistry of the in-line nucleotidyl transfer reaction.


==About this Structure==
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:15608652<ref>PMID:15608652</ref>
1XSL 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 and CAC as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/DNA-directed_DNA_polymerase DNA-directed DNA polymerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.7.7 2.7.7.7] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1XSL OCA].


==Reference==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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://ispc.weizmann.ac.il//pmbin/getpm?pmid=15608652 15608652]
</div>
[[Category: DNA-directed DNA polymerase]]
<div class="pdbe-citations 1xsl" style="background-color:#fffaf0;"></div>
 
==See Also==
*[[DNA polymerase 3D structures|DNA polymerase 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[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: CAC]]
[[Category: MG]]
[[Category: NA]]
[[Category: dna polymerase lambda]]
[[Category: helix-hairpin-helix]]
[[Category: protein-dna complex]]
 
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 20:10:24 2007''

Latest revision as of 03:40, 21 November 2024

Crystal Structure of human DNA polymerase lambda in complex with a one nucleotide DNA gapCrystal Structure of human DNA polymerase lambda in complex with a one nucleotide DNA gap

Structural highlights

1xsl is a 16 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 2.3Å
Ligands:, ,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Evolutionary Conservation

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

Publication Abstract from PubMed

Pol lambda is a family X member believed to fill short gaps during DNA repair. Here we report crystal structures of Pol lambda representing three steps in filling a single-nucleotide gap. These structures indicate that, unlike other DNA polymerases, Pol lambda does not undergo large subdomain movements during catalysis, and they provide a clear characterization of the geometry and stereochemistry of the in-line nucleotidyl transfer reaction.

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:15608652[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

See Also

References

  1. Garcia-Diaz M, Bebenek K, Krahn JM, Kunkel TA, Pedersen LC. A closed conformation for the Pol lambda catalytic cycle. Nat Struct Mol Biol. 2005 Jan;12(1):97-8. Epub 2004 Dec 19. PMID:15608652 doi:http://dx.doi.org/10.1038/nsmb876

1xsl, resolution 2.30Å

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OCA