2nrr: Difference between revisions
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'''Crystal structure of the C-terminal RNAseH endonuclase domain of UvrC''' | {{Structure | ||
|PDB= 2nrr |SIZE=350|CAPTION= <scene name='initialview01'>2nrr</scene>, resolution 1.200Å | |||
|SITE= | |||
|LIGAND= | |||
|ACTIVITY= | |||
|GENE= uvrC ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=2336 Thermotoga maritima]) | |||
}} | |||
'''Crystal structure of the C-terminal RNAseH endonuclase domain of UvrC''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
2NRR is a [ | 2NRR is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Thermotoga_maritima Thermotoga maritima]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2NRR OCA]. | ||
==Reference== | ==Reference== | ||
Structure of the C-terminal half of UvrC reveals an RNase H endonuclease domain with an Argonaute-like catalytic triad., Karakas E, Truglio JJ, Croteau D, Rhau B, Wang L, Van Houten B, Kisker C, EMBO J. 2007 Jan 24;26(2):613-22. PMID:[http:// | Structure of the C-terminal half of UvrC reveals an RNase H endonuclease domain with an Argonaute-like catalytic triad., Karakas E, Truglio JJ, Croteau D, Rhau B, Wang L, Van Houten B, Kisker C, EMBO J. 2007 Jan 24;26(2):613-22. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17245438 17245438] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Thermotoga maritima]] | [[Category: Thermotoga maritima]] | ||
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[[Category: uvrc]] | [[Category: uvrc]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 17:50:12 2008'' | ||
Revision as of 18:50, 20 March 2008
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| , resolution 1.200Å | |||||||
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| Gene: | uvrC (Thermotoga maritima) | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystal structure of the C-terminal RNAseH endonuclase domain of UvrC
OverviewOverview
Removal and repair of DNA damage by the nucleotide excision repair pathway requires two sequential incision reactions, which are achieved by the endonuclease UvrC in eubacteria. Here, we describe the crystal structure of the C-terminal half of UvrC, which contains the catalytic domain responsible for 5' incision and a helix-hairpin-helix-domain that is implicated in DNA binding. Surprisingly, the 5' catalytic domain shares structural homology with RNase H despite the lack of sequence homology and contains an uncommon DDH triad. The structure also reveals two highly conserved patches on the surface of the protein, which are not related to the active site. Mutations of residues in one of these patches led to the inability of the enzyme to bind DNA and severely compromised both incision reactions. Based on our results, we suggest a model of how UvrC forms a productive protein-DNA complex to excise the damage from DNA.
About this StructureAbout this Structure
2NRR is a Single protein structure of sequence from Thermotoga maritima. Full crystallographic information is available from OCA.
ReferenceReference
Structure of the C-terminal half of UvrC reveals an RNase H endonuclease domain with an Argonaute-like catalytic triad., Karakas E, Truglio JJ, Croteau D, Rhau B, Wang L, Van Houten B, Kisker C, EMBO J. 2007 Jan 24;26(2):613-22. PMID:17245438
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