1yd6: Difference between revisions

Revision as of 11:01, 29 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1yd6.png

Template:STRUCTURE 1yd6

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

Template:ABSTRACT PUBMED 15692561

About this StructureAbout this Structure

Full crystallographic information is available from OCA.

ReferenceReference

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

Page seeded by OCA on Tue Jul 29 11:01:43 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

@@ Line 1: / Line 1: @@
-[[Image:1yd6.gif|left|200px]]
+{{Seed}}
+[[Image:1yd6.png|left|200px]]
 <!--
@@ Line 9: / Line 10: @@
 {{STRUCTURE_1yd6|  PDB=1yd6  |  SCENE=  }}
-'''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===
-==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 31: / Line 35: @@
 [[Category: Wang, L.]]
 [[Category: Dna binding protein]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 16:10:36 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 11:01:43 2008''