2fdc

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Revision as of 07:36, 18 October 2017

Structural Basis of DNA Damage Recognition and Processing by UvrB: crystal structure of a UvrB/DNA complex

Structural highlights

2fdc is a 4 chain structure with sequence from 'bacillus caldotenax'. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Related:	1t5l, 1d9x, 1d9z, 1yd1, 1qoj
Gene:	uvrB ('Bacillus caldotenax')
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[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

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

DNA-damage recognition in the nucleotide excision repair (NER) cascade is a complex process, operating on a wide variety of damages. UvrB is the central component in prokaryotic NER, directly involved in DNA-damage recognition and guiding the DNA through repair synthesis. We report the first structure of a UvrB-double-stranded DNA complex, providing insights into the mechanism by which UvrB binds DNA, leading to formation of the preincision complex. One DNA strand, containing a 3' overhang, threads behind a beta-hairpin motif of UvrB, indicating that this motif inserts between the strands of the double helix, thereby locking down either the damaged or undamaged strand. The nucleotide directly behind the beta-hairpin is flipped out and inserted into a small, highly conserved pocket in UvrB.

Structural basis for DNA recognition and processing by UvrB.,Truglio JJ, Karakas E, Rhau B, Wang H, DellaVecchia MJ, Van Houten B, Kisker C Nat Struct Mol Biol. 2006 Apr;13(4):360-4. Epub 2006 Mar 12. PMID:16532007^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Truglio JJ, Karakas E, Rhau B, Wang H, DellaVecchia MJ, Van Houten B, Kisker C. Structural basis for DNA recognition and processing by UvrB. Nat Struct Mol Biol. 2006 Apr;13(4):360-4. Epub 2006 Mar 12. PMID:16532007 doi:10.1038/nsmb1072

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2fdc"

@@ Line 1: / Line 1: @@
 ==Structural Basis of DNA Damage Recognition and Processing by UvrB: crystal structure of a UvrB/DNA complex==
 <StructureSection load='2fdc' size='340' side='right' caption='[[2fdc]], [[Resolution|resolution]] 3.30&Aring;' scene=''>
@@ Line 6: / Line 7: @@
 <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1t5l|1t5l]], [[1d9x|1d9x]], [[1d9z|1d9z]], [[1yd1|1yd1]], [[1qoj|1qoj]]</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 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=2fdc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2fdc OCA], [http://pdbe.org/2fdc PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2fdc RCSB], [http://www.ebi.ac.uk/pdbsum/2fdc 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=2fdc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2fdc OCA], [http://pdbe.org/2fdc PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2fdc RCSB], [http://www.ebi.ac.uk/pdbsum/2fdc PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2fdc ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 29: / Line 30: @@
 </div>
 <div class="pdbe-citations 2fdc" style="background-color:#fffaf0;"></div>
-==See Also==
-*[[UvrABC|UvrABC]]
 == References ==
 <references/>

2fdc

From Proteopedia

Revision as of 07:36, 18 October 2017

Structural Basis of DNA Damage Recognition and Processing by UvrB: crystal structure of a UvrB/DNA complex

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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