1t5l
From Proteopedia
(Difference between revisions)
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1t5l]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Bacillus_caldotenax Bacillus caldotenax]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1T5L OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1T5L FirstGlance]. <br> | <table><tr><td colspan='2'>[[1t5l]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Bacillus_caldotenax Bacillus caldotenax]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1T5L OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1T5L FirstGlance]. <br> | ||
- | </td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene>< | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> |
- | <tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1d9x|1d9x]], [[1d9z|1d9z]], [[1c40|1c40]], [[1d2m|1d2m]], [[1e52|1e52]], [[1qoj|1qoj]]</td></tr> | + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1d9x|1d9x]], [[1d9z|1d9z]], [[1c40|1c40]], [[1d2m|1d2m]], [[1e52|1e52]], [[1qoj|1qoj]]</td></tr> |
- | <tr><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">UVRB ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1395 Bacillus caldotenax])</td></tr> | + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">UVRB ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1395 Bacillus caldotenax])</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=1t5l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1t5l OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1t5l RCSB], [http://www.ebi.ac.uk/pdbsum/1t5l 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=1t5l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1t5l OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1t5l RCSB], [http://www.ebi.ac.uk/pdbsum/1t5l PDBsum]</span></td></tr> |
- | <table> | + | </table> |
+ | == Function == | ||
+ | [[http://www.uniprot.org/uniprot/UVRB_BACCA UVRB_BACCA]] The UvrABC repair system catalyzes the recognition and processing of DNA lesions. A damage recognition complex composed of 2 UvrA and 2 UvrB subunits scans DNA for abnormalities. Upon binding of the UvrA(2)B(2) complex to a putative damaged site, the DNA wraps around one UvrB monomer. DNA wrap is dependent on ATP binding by UvrB and probably causes local melting of the DNA helix, facilitating insertion of UvrB beta-hairpin between the DNA strands. Then UvrB probes one DNA strand for the presence of a lesion. If a lesion is found the UvrA subunits dissociate and the UvrB-DNA preincision complex is formed. This complex is subsequently bound by UvrC and the second UvrB is released. If no lesion is found, the DNA wraps around the other UvrB subunit that will check the other stand for damage (By similarity).[HAMAP-Rule:MF_00204] | ||
== 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: Bacillus caldotenax]] | [[Category: Bacillus caldotenax]] | ||
- | [[Category: Croteau, D L | + | [[Category: Croteau, D L]] |
- | [[Category: DellaVecchia, M J | + | [[Category: DellaVecchia, M J]] |
- | [[Category: Houten, B Van | + | [[Category: Houten, B Van]] |
- | [[Category: Kisker, C | + | [[Category: Kisker, C]] |
- | [[Category: Mandavilli, B S | + | [[Category: Mandavilli, B S]] |
- | [[Category: Skorvaga, M | + | [[Category: Skorvaga, M]] |
- | [[Category: Theis, K | + | [[Category: Theis, K]] |
- | [[Category: Truglio, J J | + | [[Category: Truglio, J J]] |
[[Category: Dna damage]] | [[Category: Dna damage]] | ||
[[Category: Dna excision repair]] | [[Category: Dna excision repair]] |
Revision as of 07:30, 25 December 2014
Crystal structure of the DNA repair protein UvrB point mutant Y96A revealing a novel fold for domain 2
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Categories: Bacillus caldotenax | Croteau, D L | DellaVecchia, M J | Houten, B Van | Kisker, C | Mandavilli, B S | Skorvaga, M | Theis, K | Truglio, J J | Dna damage | Dna excision repair | Dna repair | Mfd | Ner | Nucleotide excision repair | Trcf | Uvra | Uvrb | Uvrc