2nrw

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
(New page: 200px<br /><applet load="2nrw" size="450" color="white" frame="true" align="right" spinBox="true" caption="2nrw, resolution 2.300&Aring;" /> '''Crystal structure o...)
Line 1: Line 1:
-
[[Image:2nrw.jpg|left|200px]]<br /><applet load="2nrw" size="450" color="white" frame="true" align="right" spinBox="true"
+
[[Image:2nrw.jpg|left|200px]]<br /><applet load="2nrw" size="350" color="white" frame="true" align="right" spinBox="true"
caption="2nrw, resolution 2.300&Aring;" />
caption="2nrw, resolution 2.300&Aring;" />
'''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, 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.
+
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==
-
2NRW is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Thermotoga_maritima Thermotoga maritima]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2NRW OCA].
+
2NRW is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Thermotoga_maritima Thermotoga maritima]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2NRW OCA].
==Reference==
==Reference==
Line 15: Line 15:
[[Category: Karakas, E.]]
[[Category: Karakas, E.]]
[[Category: Kisker, C.]]
[[Category: Kisker, C.]]
-
[[Category: Truglio, J.J.]]
+
[[Category: Truglio, J J.]]
[[Category: endonuclase]]
[[Category: endonuclase]]
[[Category: helix hairpin helix]]
[[Category: helix hairpin helix]]
Line 23: Line 23:
[[Category: uvrc]]
[[Category: uvrc]]
-
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 12:52:38 2007''
+
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:10:16 2008''

Revision as of 16:10, 21 February 2008

Image:2nrw.jpg

2nrw, resolution 2.300Å

Drag the structure with the mouse to rotate

Crystal structure of the C terminal half of UvrC

Overview

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

2NRW is a Single protein structure of sequence from Thermotoga maritima. Full crystallographic information is available from OCA.

Reference

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

Page seeded by OCA on Thu Feb 21 18:10:16 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2nrw"
Personal tools