|
|
| Line 3: |
Line 3: |
| | <StructureSection load='6n9l' size='340' side='right'caption='[[6n9l]], [[Resolution|resolution]] 2.01Å' scene=''> | | <StructureSection load='6n9l' size='340' side='right'caption='[[6n9l]], [[Resolution|resolution]] 2.01Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[6n9l]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_43589 Atcc 43589]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6N9L OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6N9L FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6n9l]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermotoga_maritima Thermotoga maritima]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6N9L OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6N9L FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.01Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">uvrA, TM_0480 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=2336 ATCC 43589])</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></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=6n9l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6n9l OCA], [http://pdbe.org/6n9l PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6n9l RCSB], [http://www.ebi.ac.uk/pdbsum/6n9l PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6n9l 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=6n9l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6n9l OCA], [https://pdbe.org/6n9l PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6n9l RCSB], [https://www.ebi.ac.uk/pdbsum/6n9l PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6n9l ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/UVRA_THEMA UVRA_THEMA]] The UvrABC repair system catalyzes the recognition and processing of DNA lesions. UvrA is an ATPase and a DNA-binding protein. A damage recognition complex composed of 2 UvrA and 2 UvrB subunits scans DNA for abnormalities. When the presence of a lesion has been verified by UvrB, the UvrA molecules dissociate (By similarity). | + | [https://www.uniprot.org/uniprot/UVRA_THEMA UVRA_THEMA] The UvrABC repair system catalyzes the recognition and processing of DNA lesions. UvrA is an ATPase and a DNA-binding protein. A damage recognition complex composed of 2 UvrA and 2 UvrB subunits scans DNA for abnormalities. When the presence of a lesion has been verified by UvrB, the UvrA molecules dissociate (By similarity). |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
| Line 19: |
Line 19: |
| | </div> | | </div> |
| | <div class="pdbe-citations 6n9l" style="background-color:#fffaf0;"></div> | | <div class="pdbe-citations 6n9l" style="background-color:#fffaf0;"></div> |
| | + | |
| | + | ==See Also== |
| | + | *[[UvrABC|UvrABC]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Atcc 43589]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Case, B]] | + | [[Category: Thermotoga maritima]] |
| - | [[Category: Hartley, S]] | + | [[Category: Case B]] |
| - | [[Category: Hingorani, M M]] | + | [[Category: Hartley S]] |
| - | [[Category: Jeruzalmi, D]] | + | [[Category: Hingorani MM]] |
| - | [[Category: Osuga, M]] | + | [[Category: Jeruzalmi D]] |
| - | [[Category: Adp]]
| + | [[Category: Osuga M]] |
| - | [[Category: Dna binding protein]]
| + | |
| - | [[Category: Dna damage repair]]
| + | |
| - | [[Category: Hydrolase]]
| + | |
| - | [[Category: Ner]]
| + | |
| - | [[Category: Nucleotide excision repair]]
| + | |
| - | [[Category: Uvra]]
| + | |
| Structural highlights
Function
UVRA_THEMA The UvrABC repair system catalyzes the recognition and processing of DNA lesions. UvrA is an ATPase and a DNA-binding protein. A damage recognition complex composed of 2 UvrA and 2 UvrB subunits scans DNA for abnormalities. When the presence of a lesion has been verified by UvrB, the UvrA molecules dissociate (By similarity).
Publication Abstract from PubMed
The UvrA2 dimer finds lesions in DNA and initiates nucleotide excision repair. Each UvrA monomer contains two essential ATPase sites: proximal (P) and distal (D). The manner whereby their activities enable UvrA2 damage sensing and response remains to be clarified. We report three key findings from the first pre-steady state kinetic analysis of each site. Absent DNA, a P2ATP-D2ADP species accumulates when the low-affinity proximal sites bind ATP and enable rapid ATP hydrolysis and phosphate release by the high-affinity distal sites, and ADP release limits catalytic turnover. Native DNA stimulates ATP hydrolysis by all four sites, causing UvrA2 to transition through a different species, P2ADP-D2ADP. Lesion-containing DNA changes the mechanism again, suppressing ATP hydrolysis by the proximal sites while distal sites cycle through hydrolysis and ADP release, to populate proximal ATP-bound species, P2ATP-Dempty and P2ATP-D2ATP. Thus, damaged and native DNA trigger distinct ATPase site activities, which could explain why UvrA2 forms stable complexes with UvrB on damaged DNA compared with weaker, more dynamic complexes on native DNA. Such specific coupling between the DNA substrate and the ATPase mechanism of each site provides new insights into how UvrA2 utilizes ATP for lesion search, recognition and repair.
The ATPase mechanism of UvrA2 reveals the distinct roles of proximal and distal ATPase sites in nucleotide excision repair.,Case BC, Hartley S, Osuga M, Jeruzalmi D, Hingorani MM Nucleic Acids Res. 2019 Mar 20. pii: 5403497. doi: 10.1093/nar/gkz180. PMID:30892613[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Case BC, Hartley S, Osuga M, Jeruzalmi D, Hingorani MM. The ATPase mechanism of UvrA2 reveals the distinct roles of proximal and distal ATPase sites in nucleotide excision repair. Nucleic Acids Res. 2019 Mar 20. pii: 5403497. doi: 10.1093/nar/gkz180. PMID:30892613 doi:http://dx.doi.org/10.1093/nar/gkz180
|
