 |
PDBsum entry 3v4r
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
 |
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
Hydrolase/DNA
|
PDB id
|
|
|
|
3v4r
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
PDB id:
|
|
|
|
| Name: |
|
Hydrolase/DNA
|
|
|
Title:
|
|
Crystal structure of a uvrb dimer-DNA complex
|
|
Structure:
|
|
Uvrabc system protein b. Chain: a, b. Synonym: protein uvrb, excinuclease abc subunit b, protein dina. Engineered: yes. Dna: 5 -tactgttt-3. Chain: c, d. Engineered: yes
|
|
Source:
|
|
Bacillus subtilis. Organism_taxid: 1423. Gene: bsu35170, dina, uvr, uvrb. Expressed in: escherichia coli. Expression_system_taxid: 469008. Synthetic: yes. Other_details: synthesised DNA
|
|
Resolution:
|
|
|
3.25Å
|
R-factor:
|
0.182
|
R-free:
|
0.219
|
|
|
Authors:
|
|
M.P.J.Webster,R.Jukes,T.Barrett
|
|
Key ref:
|
|
M.P.Webster
et al.
(2012).
Crystal structure of the UvrB dimer: insights into the nature and functioning of the UvrAB damage engagement and UvrB-DNA complexes.
Nucleic Acids Res,
40,
8743-8758.
PubMed id:
|
|
|
Date:
|
|
|
15-Dec-11
|
Release date:
|
04-Jul-12
|
|
|
|
|
|
|
PROCHECK
|
|
|
|
|
|
Headers
|
|
|
|
References
|
|
|
|
|
|
|
|
P37954
(UVRB_BACSU) -
UvrABC system protein B from Bacillus subtilis (strain 168)
|
|
|
|
Seq:
Struc:
|
|
|
|
661 a.a.
586 a.a.
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
Key: |
|
 |
Secondary structure |
|
 |
CATH domain |
|
|
|
|
|
|
|
|
|
|
|
|
A-C-T-G-T-T-T
7 bases
|
|
|
|
A-C-T-G-T-T-T
7 bases
|
|
|
|
|
|
|
|
|
|
|
|
|
|
Enzyme class:
|
|
E.C.3.1.21.5
- type Iii site-specific deoxyribonuclease.
|
|
|
|
|
|
|
Reaction:
|
|
Endonucleolytic cleavage of DNA to give specific double-stranded fragments with terminal 5'-phosphates.
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
 |
|
|
|
|
|
|
| |
|
|
Nucleic Acids Res
40:8743-8758
(2012)
|
|
PubMed id:
|
|
|
|
|
|
| |
|
Crystal structure of the UvrB dimer: insights into the nature and functioning of the UvrAB damage engagement and UvrB-DNA complexes.
|
|
M.P.Webster,
R.Jukes,
V.S.Zamfir,
C.W.Kay,
C.Bagnéris,
T.Barrett.
|
|
|
|
|
| |
ABSTRACT
|
|
|
|
| |
|
|
UvrB has a central role in the highly conserved UvrABC pathway functioning not
only as a damage recognition element but also as an essential component of the
lesion tracking machinery. While it has been recently confirmed that the
tracking assembly comprises a UvrA(2)B(2) heterotetramer, the configurations of
the damage engagement and UvrB-DNA handover complexes remain obscure. Here, we
present the first crystal structure of a UvrB dimer whose biological
significance has been verified using both chemical cross-linking and electron
paramagnetic resonance spectroscopy. We demonstrate that this dimeric species
stably associates with UvrA and forms a UvrA(2)B(2)-DNA complex. Our studies
also illustrate how signals are transduced between the ATP and DNA binding sites
to generate the helicase activity pivotal to handover and formation of the
UvrB(2)-DNA complex, providing key insights into the configurations of these
important repair intermediates.
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
 |
 |
 |
|
Links
