3ux8: Difference between revisions

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<StructureSection load='3ux8' size='340' side='right'caption='[[3ux8]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
<StructureSection load='3ux8' size='340' side='right'caption='[[3ux8]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[3ux8]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Geos2 Geos2]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3UX8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3UX8 FirstGlance]. <br>
<table><tr><td colspan='2'>[[3ux8]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Geobacillus_sp._Y412MC52 Geobacillus sp. Y412MC52]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3UX8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3UX8 FirstGlance]. <br>
</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>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.1&#8491;</td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">GYMC52_3203, uvrA ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=550542 GEOS2])</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'>[https://proteopedia.org/fgij/fg.htm?mol=3ux8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ux8 OCA], [https://pdbe.org/3ux8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3ux8 RCSB], [https://www.ebi.ac.uk/pdbsum/3ux8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3ux8 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=3ux8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ux8 OCA], [https://pdbe.org/3ux8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3ux8 RCSB], [https://www.ebi.ac.uk/pdbsum/3ux8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3ux8 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[https://www.uniprot.org/uniprot/E8SW61_GEOS2 E8SW61_GEOS2]] 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).[HAMAP-Rule:MF_00205]  
[https://www.uniprot.org/uniprot/A0A0E0TG05_GEOS2 A0A0E0TG05_GEOS2] 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.[HAMAP-Rule:MF_00205]
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Nucleotide excision repair (NER) is used by all organisms to eliminate DNA lesions. We determined the structure of the Geobacillus stearothermophilus UvrA-UvrB complex, the damage-sensor in bacterial NER and a new structure of UvrA. We observe that the DNA binding surface of UvrA, previously found in an open shape that binds damaged DNA, also exists in a closed groove shape compatible with native DNA only. The sensor contains two UvrB molecules that flank the UvrA dimer along the predicted path for DNA, ~80 A from the lesion. We show that the conserved signature domain II of UvrA mediates a nexus of contacts among UvrA, UvrB and DNA. Further, in our new structure of UvrA, this domain adopts an altered conformation while an adjacent nucleotide binding site is vacant. Our findings raise unanticipated questions about NER and also suggest a revised picture of its early stages.
 
Structure and mechanism of the UvrA-UvrB DNA damage sensor.,Pakotiprapha D, Samuels M, Shen K, Hu JH, Jeruzalmi D Nat Struct Mol Biol. 2012 Feb 5;19(3):291-8. doi: 10.1038/nsmb.2240. PMID:22307053<ref>PMID:22307053</ref>
 
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 3ux8" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==
*[[UvrABC|UvrABC]]
*[[UvrABC|UvrABC]]
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Geos2]]
[[Category: Geobacillus sp. Y412MC52]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Jeruzalmi, D]]
[[Category: Jeruzalmi D]]
[[Category: Pakotiprapha, D]]
[[Category: Pakotiprapha D]]
[[Category: Samuels, M A]]
[[Category: Samuels MA]]
[[Category: Abc atpase]]
[[Category: Dna]]
[[Category: Dna binding protein]]
[[Category: Dna repair]]
[[Category: Nucleotide excision repair]]
[[Category: Uvra]]

Latest revision as of 13:29, 1 March 2024

Crystal structure of UvrACrystal structure of UvrA

Structural highlights

3ux8 is a 1 chain structure with sequence from Geobacillus sp. Y412MC52. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.1Å
Ligands:,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

A0A0E0TG05_GEOS2 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.[HAMAP-Rule:MF_00205]

See Also

3ux8, resolution 2.10Å

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