1t5l: Difference between revisions

Revision as of 14:31, 28 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1t5l.png

Template:STRUCTURE 1t5l

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

Template:ABSTRACT PUBMED 15192705

About this StructureAbout this Structure

1T5L is a Single protein structure of sequence from Bacillus caldotenax. Full crystallographic information is available from OCA.

ReferenceReference

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

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OCA

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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===
-==Overview==
+<!--
-Nucleotide excision repair (NER) is a highly conserved DNA repair mechanism present in all kingdoms of life. UvrB is a central component of the bacterial NER system, participating in damage recognition, strand excision and repair synthesis. None of the three presently available crystal structures of UvrB has defined the structure of domain 2, which is critical for the interaction with UvrA. We have solved the crystal structure of the UvrB Y96A variant, which reveals a new fold for domain 2 and identifies highly conserved residues located on its surface. These residues are restricted to the face of UvrB important for DNA binding and may be critical for the interaction of UvrB with UvrA. We have mutated these residues to study their role in the incision reaction, formation of the pre-incision complex, destabilization of short duplex regions in DNA, binding to UvrA and ATP hydrolysis. Based on the structural and biochemical data, we conclude that domain 2 is required for a productive UvrA-UvrB interaction, which is a pre-requisite for all subsequent steps in nucleotide excision repair.
+The line below this paragraph, {{ABSTRACT_PUBMED_15192705}}, adds the Publication Abstract to the page
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+{{ABSTRACT_PUBMED_15192705}}
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