1t5l
From Proteopedia
(New page: 200px<br /><applet load="1t5l" size="450" color="white" frame="true" align="right" spinBox="true" caption="1t5l, resolution 2.60Å" /> '''Crystal structure of...) |
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| - | [[Image:1t5l.gif|left|200px]]<br /><applet load="1t5l" size=" | + | [[Image:1t5l.gif|left|200px]]<br /><applet load="1t5l" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1t5l, resolution 2.60Å" /> | caption="1t5l, resolution 2.60Å" /> | ||
'''Crystal structure of the DNA repair protein UvrB point mutant Y96A revealing a novel fold for domain 2'''<br /> | '''Crystal structure of the DNA repair protein UvrB point mutant Y96A revealing a novel fold for domain 2'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Nucleotide excision repair (NER) is a highly conserved DNA repair | + | 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. |
==About this Structure== | ==About this Structure== | ||
| - | 1T5L is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_caldotenax Bacillus caldotenax] with ZN as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | + | 1T5L is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_caldotenax Bacillus caldotenax] with <scene name='pdbligand=ZN:'>ZN</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1T5L OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Bacillus caldotenax]] | [[Category: Bacillus caldotenax]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Croteau, D | + | [[Category: Croteau, D L.]] |
| - | [[Category: DellaVecchia, M | + | [[Category: DellaVecchia, M J.]] |
| - | [[Category: Houten, B | + | [[Category: Houten, B Van.]] |
[[Category: Kisker, C.]] | [[Category: Kisker, C.]] | ||
| - | [[Category: Mandavilli, B | + | [[Category: Mandavilli, B S.]] |
[[Category: Skorvaga, M.]] | [[Category: Skorvaga, M.]] | ||
[[Category: Theis, K.]] | [[Category: Theis, K.]] | ||
| - | [[Category: Truglio, J | + | [[Category: Truglio, J J.]] |
[[Category: ZN]] | [[Category: ZN]] | ||
[[Category: crystallography]] | [[Category: crystallography]] | ||
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[[Category: uvrc]] | [[Category: uvrc]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:10:07 2008'' |
Revision as of 13:10, 21 February 2008
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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.
About this Structure
1T5L is a Single protein structure of sequence from Bacillus caldotenax with as ligand. Full crystallographic information is available from OCA.
Reference
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
Page seeded by OCA on Thu Feb 21 15:10:07 2008
Categories: Bacillus caldotenax | Single protein | Croteau, D L. | DellaVecchia, M J. | Houten, B Van. | Kisker, C. | Mandavilli, B S. | Skorvaga, M. | Theis, K. | Truglio, J J. | ZN | Crystallography | Dna damage | Dna repair | Mfd | Ner | Nucleotide excision repair | Trcf | Uvra | Uvrb | Uvrc
