1t5l

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{{Seed}}
 
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[[Image:1t5l.png|left|200px]]
 
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{{STRUCTURE_1t5l| PDB=1t5l | SCENE= }}
{{STRUCTURE_1t5l| PDB=1t5l | SCENE= }}
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===Crystal structure of the DNA repair protein UvrB point mutant Y96A revealing a novel fold for domain 2===
===Crystal structure of the DNA repair protein UvrB point mutant Y96A revealing a novel fold for domain 2===
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{{ABSTRACT_PUBMED_15192705}}
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==Function==
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[[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]
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(as it appears on PubMed at http://www.pubmed.gov), where 15192705 is the PubMed ID number.
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{{ABSTRACT_PUBMED_15192705}}
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==About this Structure==
==About this Structure==
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1T5L is a 2 chains structure of sequences 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].
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[[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].
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==See Also==
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*[[UvrABC|UvrABC]]
==Reference==
==Reference==
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<ref group="xtra">PMID:15192705</ref><references group="xtra"/>
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<ref group="xtra">PMID:015192705</ref><references group="xtra"/><references/>
[[Category: Bacillus caldotenax]]
[[Category: Bacillus caldotenax]]
[[Category: Croteau, D L.]]
[[Category: Croteau, D L.]]
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[[Category: Theis, K.]]
[[Category: Theis, K.]]
[[Category: Truglio, J J.]]
[[Category: Truglio, J J.]]
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[[Category: Crystallography]]
 
[[Category: Dna damage]]
[[Category: Dna damage]]
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[[Category: Dna excision repair]]
[[Category: Dna repair]]
[[Category: Dna repair]]
[[Category: Mfd]]
[[Category: Mfd]]
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[[Category: Uvrb]]
[[Category: Uvrb]]
[[Category: Uvrc]]
[[Category: Uvrc]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Feb 17 10:37:37 2009''
 

Revision as of 08:41, 23 April 2014

Template:STRUCTURE 1t5l

Contents

Crystal structure of the DNA repair protein UvrB point mutant Y96A revealing a novel fold for domain 2

Template:ABSTRACT PUBMED 15192705

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]

About this Structure

1t5l is a 2 chain structure with sequence from Bacillus caldotenax. Full crystallographic information is available from OCA.

See Also

Reference

  • Truglio JJ, Croteau DL, Skorvaga M, DellaVecchia MJ, Theis K, Mandavilli BS, Van Houten B, Kisker C. Interactions between UvrA and UvrB: the role of UvrB's domain 2 in nucleotide excision repair. EMBO J. 2004 Jul 7;23(13):2498-509. Epub 2004 Jun 10. PMID:15192705 doi:10.1038/sj.emboj.7600263

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