1yd2: Difference between revisions

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[[Image:1yd2.~~gif~~|left|200px]]

[[Image:1yd2.png|left|200px]]

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~~'''~~Crystal structure of the GIY-YIG N-terminal endonuclease domain of UvrC from Thermotoga maritima: Point mutant Y19F bound to the catalytic divalent cation~~'''~~

===Crystal structure of the GIY-YIG N-terminal endonuclease domain of UvrC from Thermotoga maritima: Point mutant Y19F bound to the catalytic divalent cation===

~~==Overview==~~

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~~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.~~

The line below this paragraph, {{ABSTRACT_PUBMED_15692561}}, adds the Publication Abstract to the page

(as it appears on PubMed at http://www.pubmed.gov), where 15692561 is the PubMed ID number.

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==About this Structure==

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[[Category: Wang, L.]]

[[Category: Dna binding protein]]

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Sat May 3 16~~:10:16 2008''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 23:30:48 2008''

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-[[Image:1yd2.gif|left|200px]]
+{{Seed}}
+[[Image:1yd2.png|left|200px]]
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 {{STRUCTURE_1yd2|  PDB=1yd2  |  SCENE=  }}
-'''Crystal structure of the GIY-YIG N-terminal endonuclease domain of UvrC from Thermotoga maritima: Point mutant Y19F bound to the catalytic divalent cation'''
+===Crystal structure of the GIY-YIG N-terminal endonuclease domain of UvrC from Thermotoga maritima: Point mutant Y19F bound to the catalytic divalent cation===
-==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.
+The line below this paragraph, {{ABSTRACT_PUBMED_15692561}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 15692561 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_15692561}}
 ==About this Structure==
@@ Line 33: / Line 37: @@
 [[Category: Wang, L.]]
 [[Category: Dna binding protein]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 16:10:16 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 23:30:48 2008''