2nrt: Difference between revisions
New page: left|200px<br /><applet load="2nrt" size="450" color="white" frame="true" align="right" spinBox="true" caption="2nrt, resolution 1.500Å" /> '''Crystal structure o... |
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[[Image:2nrt.jpg|left|200px]]<br /><applet load="2nrt" size=" | [[Image:2nrt.jpg|left|200px]]<br /><applet load="2nrt" size="350" color="white" frame="true" align="right" spinBox="true" | ||
caption="2nrt, resolution 1.500Å" /> | caption="2nrt, resolution 1.500Å" /> | ||
'''Crystal structure of the C-terminal half of UvrC'''<br /> | '''Crystal structure of the C-terminal half of UvrC'''<br /> | ||
==Overview== | ==Overview== | ||
Removal and repair of DNA damage by the nucleotide excision repair pathway | 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 Structure== | ==About this Structure== | ||
2NRT is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Thermotoga_maritima Thermotoga maritima] with CL as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | 2NRT is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Thermotoga_maritima Thermotoga maritima] with <scene name='pdbligand=CL:'>CL</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2NRT OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: Karakas, E.]] | [[Category: Karakas, E.]] | ||
[[Category: Kisker, C.]] | [[Category: Kisker, C.]] | ||
[[Category: Truglio, J | [[Category: Truglio, J J.]] | ||
[[Category: CL]] | [[Category: CL]] | ||
[[Category: endonuclease]] | [[Category: endonuclease]] | ||
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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 18:10:12 2008'' | ||
Revision as of 19:10, 21 February 2008
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Crystal structure of the C-terminal half 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
2NRT is a Single protein structure of sequence from Thermotoga maritima with as ligand. 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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