1jih: Difference between revisions
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1jih]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JIH OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1JIH FirstGlance]. <br> | <table><tr><td colspan='2'>[[1jih]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JIH OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1JIH FirstGlance]. <br> | ||
</td></tr><tr><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">RAD30 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 Saccharomyces cerevisiae])</td></tr> | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">RAD30 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 Saccharomyces cerevisiae])</td></tr> | ||
<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1jih FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1jih OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1jih RCSB], [http://www.ebi.ac.uk/pdbsum/1jih PDBsum]</span></td></tr> | <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=1jih FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1jih OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1jih RCSB], [http://www.ebi.ac.uk/pdbsum/1jih PDBsum]</span></td></tr> | ||
<table> | </table> | ||
== Function == | |||
[[http://www.uniprot.org/uniprot/POLH_YEAST POLH_YEAST]] 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. Plays an important role in the repair of UV-induced pyrimidine dimers. Depending on the context, it inserts the correct base, but causes frequent base transitions and transversions. Efficiently incorporates nucleotides opposite to other UV or oxidative DNA damages like O(6)-methylguanine, 7,8-dihydro-8-oxoguanine, 2,6-diamino-4-hydroxy-5-formamidopyrimidine of 2'-deoxyguanosine (FaPydG), or p-benzoquinone DNA adducts.<ref>PMID:9409821</ref> <ref>PMID:10347143</ref> <ref>PMID:10601233</ref> <ref>PMID:9974380</ref> <ref>PMID:10924462</ref> <ref>PMID:10713149</ref> <ref>PMID:11027270</ref> <ref>PMID:10932195</ref> <ref>PMID:10725365</ref> <ref>PMID:11062246</ref> <ref>PMID:11545742</ref> <ref>PMID:11113193</ref> <ref>PMID:11238937</ref> <ref>PMID:11054429</ref> <ref>PMID:12110599</ref> <ref>PMID:11861920</ref> <ref>PMID:12899630</ref> <ref>PMID:12665597</ref> <ref>PMID:12888515</ref> <ref>PMID:12692307</ref> <ref>PMID:14527996</ref> <ref>PMID:15157108</ref> <ref>PMID:15544332</ref> <ref>PMID:15284331</ref> <ref>PMID:15333698</ref> <ref>PMID:15024063</ref> <ref>PMID:15779911</ref> <ref>PMID:16181813</ref> <ref>PMID:15520252</ref> <ref>PMID:16366567</ref> <ref>PMID:15743815</ref> <ref>PMID:16866379</ref> <ref>PMID:16387871</ref> <ref>PMID:16415180</ref> | |||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Saccharomyces cerevisiae]] | [[Category: Saccharomyces cerevisiae]] | ||
[[Category: Aggarwal, A K | [[Category: Aggarwal, A K]] | ||
[[Category: Escalante, C R | [[Category: Escalante, C R]] | ||
[[Category: Johnson, R E | [[Category: Johnson, R E]] | ||
[[Category: Prakash, L | [[Category: Prakash, L]] | ||
[[Category: Prakash, S | [[Category: Prakash, S]] | ||
[[Category: Trincao, J | [[Category: Trincao, J]] | ||
[[Category: Dna polymerase]] | [[Category: Dna polymerase]] | ||
[[Category: Translation]] | [[Category: Translation]] | ||
[[Category: Translesion]] | [[Category: Translesion]] | ||
[[Category: Yeast]] | [[Category: Yeast]] |
Revision as of 09:45, 25 December 2014
Yeast DNA Polymerase ETAYeast DNA Polymerase ETA
Structural highlights
Function[POLH_YEAST] 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. Plays an important role in the repair of UV-induced pyrimidine dimers. Depending on the context, it inserts the correct base, but causes frequent base transitions and transversions. Efficiently incorporates nucleotides opposite to other UV or oxidative DNA damages like O(6)-methylguanine, 7,8-dihydro-8-oxoguanine, 2,6-diamino-4-hydroxy-5-formamidopyrimidine of 2'-deoxyguanosine (FaPydG), or p-benzoquinone DNA adducts.[1] [2] [3] [4] [5] [6] [7] [8] [9] [10] [11] [12] [13] [14] [15] [16] [17] [18] [19] [20] [21] [22] [23] [24] [25] [26] [27] [28] [29] [30] [31] [32] [33] [34] 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 PubMedDNA polymerase eta is unique among eukaryotic polymerases in its proficient ability to replicate through a variety of distorting DNA lesions. We report here the crystal structure of the catalytic core of S. cerevisiae DNA polymerase eta, determined at 2.25A resolution. The structure reveals a novel polydactyl right hand-shaped molecule with a unique polymerase-associated domain. We identify the catalytic residues and show that the fingers and thumb domains are unusually small and stubby. In particular, the unexpected absence of helices "O" and "O1" in the fingers domain suggests that openness of the active site is the critical feature which enables DNA polymerase eta to replicate through DNA lesions such as a UV-induced cis-syn thymine-thymine dimer. Structure of the catalytic core of S. cerevisiae DNA polymerase eta: implications for translesion DNA synthesis.,Trincao J, Johnson RE, Escalante CR, Prakash S, Prakash L, Aggarwal AK Mol Cell. 2001 Aug;8(2):417-26. PMID:11545743[35] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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