4u6p

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'''Unreleased structure'''
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==Structural mechanism of error-free bypass of major benzo[a]pyrene adduct by human polymerase kappa==
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<StructureSection load='4u6p' size='340' side='right' caption='[[4u6p]], [[Resolution|resolution]] 2.59&Aring;' scene=''>
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The entry 4u6p is ON HOLD
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== Structural highlights ==
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<table><tr><td colspan='2'>[[4u6p]] is a 6 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4U6P OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4U6P FirstGlance]. <br>
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Authors: Jha, V.K., Ling, H.
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=DCT:2,3-DIDEOXYCYTIDINE+5-TRIPHOSPHATE'>DCT</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=PGE:TRIETHYLENE+GLYCOL'>PGE</scene></td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4u7c|4u7c]]</td></tr>
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Description: Structural mechanism of error-free bypass of major benzo[a]pyrene adduct by human polymerase kappa
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<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[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] </span></td></tr>
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[[Category: Unreleased Structures]]
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4u6p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4u6p OCA], [http://pdbe.org/4u6p PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4u6p RCSB], [http://www.ebi.ac.uk/pdbsum/4u6p PDBsum]</span></td></tr>
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[[Category: Jha, V.K]]
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</table>
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== Function ==
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[[http://www.uniprot.org/uniprot/POLK_HUMAN POLK_HUMAN]] DNA polymerase specifically involved in DNA repair. Plays an important role in translesion synthesis, where the normal high-fidelity DNA polymerases cannot proceed and DNA synthesis stalls. Depending on the context, it inserts the correct base, but causes frequent base transitions, transversions and frameshifts. Lacks 3'-5' proofreading exonuclease activity. Forms a Schiff base with 5'-deoxyribose phosphate at abasic sites, but does not have lyase activity.<ref>PMID:10620008</ref> <ref>PMID:11024016</ref> <ref>PMID:12145297</ref> <ref>PMID:12444249</ref> <ref>PMID:12952891</ref> <ref>PMID:14630940</ref> <ref>PMID:15533436</ref>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: DNA-directed DNA polymerase]]
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[[Category: Jha, V K]]
[[Category: Ling, H]]
[[Category: Ling, H]]
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[[Category: Dna damage tolerance]]
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[[Category: Dna replication]]
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[[Category: Environment pollution]]
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[[Category: Polymerase kappa]]
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[[Category: Transferase-dna complex]]

Revision as of 02:26, 28 January 2016

Structural mechanism of error-free bypass of major benzo[a]pyrene adduct by human polymerase kappa

4u6p, resolution 2.59Å

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