1yd6: Difference between revisions
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==Crystal structure of the GIY-YIG N-terminal endonuclease domain of UvrC from Bacillus caldotenax== | ==Crystal structure of the GIY-YIG N-terminal endonuclease domain of UvrC from Bacillus caldotenax== | ||
<StructureSection load='1yd6' size='340' side='right' caption='[[1yd6]], [[Resolution|resolution]] 2.00Å' scene=''> | <StructureSection load='1yd6' size='340' side='right'caption='[[1yd6]], [[Resolution|resolution]] 2.00Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1yd6]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_caldotenax"_heinen_and_heinen_1972 "bacillus caldotenax" heinen and heinen 1972]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1YD6 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1YD6 FirstGlance]. <br> | <table><tr><td colspan='2'>[[1yd6]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_caldotenax"_heinen_and_heinen_1972 "bacillus caldotenax" heinen and heinen 1972]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1YD6 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1YD6 FirstGlance]. <br> | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Bacillus caldotenax heinen and heinen 1972]] | [[Category: Bacillus caldotenax heinen and heinen 1972]] | ||
[[Category: Large Structures]] | |||
[[Category: Croteau, D L]] | [[Category: Croteau, D L]] | ||
[[Category: DellaVecchia, M J]] | [[Category: DellaVecchia, M J]] | ||
Revision as of 20:17, 29 January 2020
Crystal structure of the GIY-YIG N-terminal endonuclease domain of UvrC from Bacillus caldotenaxCrystal structure of the GIY-YIG N-terminal endonuclease domain of UvrC from Bacillus caldotenax
Structural highlights
Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedNucleotide 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. 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences |
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