1k1q

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Current revision (07:43, 7 February 2024) (edit) (undo)
 
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<StructureSection load='1k1q' size='340' side='right'caption='[[1k1q]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
<StructureSection load='1k1q' size='340' side='right'caption='[[1k1q]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[1k1q]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Atcc_35091 Atcc 35091]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1K1Q OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1K1Q FirstGlance]. <br>
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<table><tr><td colspan='2'>[[1k1q]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharolobus_solfataricus Saccharolobus solfataricus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1K1Q OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1K1Q FirstGlance]. <br>
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</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1k1s|1k1s]]</div></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.8&#8491;</td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">DBH ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=2287 ATCC 35091])</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1k1q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1k1q OCA], [https://pdbe.org/1k1q PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1k1q RCSB], [https://www.ebi.ac.uk/pdbsum/1k1q PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1k1q ProSAT]</span></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=1k1q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1k1q OCA], [https://pdbe.org/1k1q PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1k1q RCSB], [https://www.ebi.ac.uk/pdbsum/1k1q PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1k1q ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[https://www.uniprot.org/uniprot/DPO4_SULSF DPO4_SULSF]] Poorly processive, error-prone DNA polymerase involved in untargeted mutagenesis. Copies undamaged DNA at stalled replication forks, which arise in vivo from mismatched or misaligned primer ends. These misaligned primers can be extended by PolIV. Exhibits no 3'-5' exonuclease (proofreading) activity. May be involved in translesional synthesis.
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[https://www.uniprot.org/uniprot/DPO4_SACSO DPO4_SACSO] Poorly processive, error-prone DNA polymerase involved in untargeted mutagenesis. Copies undamaged DNA at stalled replication forks, which arise in vivo from mismatched or misaligned primer ends. These misaligned primers can be extended by PolIV. Exhibits no 3'-5' exonuclease (proofreading) activity. May be involved in translesional synthesis.
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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</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=1k1q 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=1k1q ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
 
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== Publication Abstract from PubMed ==
 
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A new group of error-prone DNA polymerases overcomes the blockage posed to normal DNA replication by damaged template bases, suggesting an active site with a loose, flexible pocket that accommodates aberrant DNA structures. We have determined a 2.8 A resolution crystal structure of the Sulfolobus solfataricus Dbh protein, a DNA translesion polymerase closely related to Escherichia coli DNA polymerase IV and human polymerase kappa. A high error rate is observed for the Dbh polymerase in a range of 10(-2)-10(-3) for all 12 base substitution mispairs. The crystal structure of Dbh reveals an overall architecture resembling other DNA polymerases but has unique features that are likely to contribute to error-prone synthesis, including -1 frameshifting mutations.
 
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Crystal structure of a DinB family error-prone DNA polymerase from Sulfolobus solfataricus.,Silvian LF, Toth EA, Pham P, Goodman MF, Ellenberger T Nat Struct Biol. 2001 Nov;8(11):984-9. PMID:11685247<ref>PMID:11685247</ref>
 
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 
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</div>
 
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<div class="pdbe-citations 1k1q" style="background-color:#fffaf0;"></div>
 
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== References ==
 
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<references/>
 
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Atcc 35091]]
 
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Ellenberger, T]]
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[[Category: Saccharolobus solfataricus]]
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[[Category: Goodman, M F]]
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[[Category: Ellenberger T]]
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[[Category: Pham, P]]
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[[Category: Goodman MF]]
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[[Category: Silvian, L F]]
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[[Category: Pham P]]
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[[Category: Toth, E A]]
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[[Category: Silvian LF]]
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[[Category: Dna polymerase]]
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[[Category: Toth EA]]
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[[Category: Error-prone polymerase]]
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[[Category: Lesion-bypass polymerase]]
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[[Category: Transcription]]
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Current revision

Crystal Structure of a DinB Family Error Prone DNA Polymerase from Sulfolobus solfataricus

PDB ID 1k1q

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