1yd6
From Proteopedia
(New page: 200px<br /><applet load="1yd6" size="450" color="white" frame="true" align="right" spinBox="true" caption="1yd6, resolution 2.00Å" /> '''Crystal structure of...) |
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| - | [[Image:1yd6.gif|left|200px]]<br /><applet load="1yd6" size=" | + | [[Image:1yd6.gif|left|200px]]<br /><applet load="1yd6" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1yd6, resolution 2.00Å" /> | caption="1yd6, resolution 2.00Å" /> | ||
'''Crystal structure of the GIY-YIG N-terminal endonuclease domain of UvrC from Bacillus caldotenax'''<br /> | '''Crystal structure of the GIY-YIG N-terminal endonuclease domain of UvrC from Bacillus caldotenax'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Nucleotide excision repair is a highly conserved DNA repair mechanism | + | Nucleotide excision repair is a highly conserved DNA repair mechanism present in all kingdoms of life. The incision reaction is a critical step for damage removal and is accomplished by the UvrC protein in eubacteria. No structural information is so far available for the 3' incision reaction. Here we report the crystal structure of the N-terminal catalytic domain of UvrC at 1.5 A resolution, which catalyzes the 3' incision reaction and shares homology with the catalytic domain of the GIY-YIG family of intron-encoded homing endonucleases. The structure reveals a patch of highly conserved residues surrounding a catalytic magnesium-water cluster, suggesting that the metal binding site is an essential feature of UvrC and all GIY-YIG endonuclease domains. Structural and biochemical data strongly suggest that the N-terminal endonuclease domain of UvrC utilizes a novel one-metal mechanism to cleave the phosphodiester bond. |
==About this Structure== | ==About this Structure== | ||
| - | 1YD6 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Bacillus_caldotenax Bacillus caldotenax] with CL and SO4 as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | + | 1YD6 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Bacillus_caldotenax Bacillus caldotenax] with <scene name='pdbligand=CL:'>CL</scene> and <scene name='pdbligand=SO4:'>SO4</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1YD6 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Bacillus caldotenax]] | [[Category: Bacillus caldotenax]] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
| - | [[Category: Croteau, D | + | [[Category: Croteau, D L.]] |
| - | [[Category: DellaVecchia, M | + | [[Category: DellaVecchia, M J.]] |
| - | [[Category: Houten, B | + | [[Category: Houten, B Van.]] |
[[Category: Karakas, E.]] | [[Category: Karakas, E.]] | ||
[[Category: Kisker, C.]] | [[Category: Kisker, C.]] | ||
[[Category: Rhau, B.]] | [[Category: Rhau, B.]] | ||
[[Category: Skorvaga, M.]] | [[Category: Skorvaga, M.]] | ||
| - | [[Category: Truglio, J | + | [[Category: Truglio, J J.]] |
[[Category: Wang, H.]] | [[Category: Wang, H.]] | ||
[[Category: Wang, L.]] | [[Category: Wang, L.]] | ||
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[[Category: dna binding protein]] | [[Category: dna binding protein]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:04:05 2008'' |
Revision as of 14:04, 21 February 2008
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Crystal structure of the GIY-YIG N-terminal endonuclease domain of UvrC from Bacillus caldotenax
Overview
Nucleotide excision repair is a highly conserved DNA repair mechanism present in all kingdoms of life. The incision reaction is a critical step for damage removal and is accomplished by the UvrC protein in eubacteria. No structural information is so far available for the 3' incision reaction. Here we report the crystal structure of the N-terminal catalytic domain of UvrC at 1.5 A resolution, which catalyzes the 3' incision reaction and shares homology with the catalytic domain of the GIY-YIG family of intron-encoded homing endonucleases. The structure reveals a patch of highly conserved residues surrounding a catalytic magnesium-water cluster, suggesting that the metal binding site is an essential feature of UvrC and all GIY-YIG endonuclease domains. Structural and biochemical data strongly suggest that the N-terminal endonuclease domain of UvrC utilizes a novel one-metal mechanism to cleave the phosphodiester bond.
About this Structure
1YD6 is a Protein complex structure of sequences from Bacillus caldotenax with and as ligands. Full crystallographic information is available from OCA.
Reference
Structural insights into the first incision reaction during nucleotide excision repair., Truglio JJ, Rhau B, Croteau DL, Wang L, Skorvaga M, Karakas E, DellaVecchia MJ, Wang H, Van Houten B, Kisker C, EMBO J. 2005 Mar 9;24(5):885-94. Epub 2005 Feb 3. PMID:15692561
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