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2nrz

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[[Image:2nrz.jpg|left|200px]]
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{{STRUCTURE_2nrz| PDB=2nrz | SCENE= }}
{{STRUCTURE_2nrz| PDB=2nrz | SCENE= }}
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'''Crystal structure of the C-terminal half of UvrC bound to its catalytic divalent cation'''
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===Crystal structure of the C-terminal half of UvrC bound to its catalytic divalent cation===
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==Overview==
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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.
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(as it appears on PubMed at http://www.pubmed.gov), where 17245438 is the PubMed ID number.
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{{ABSTRACT_PUBMED_17245438}}
==About this Structure==
==About this Structure==
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[[Category: Uvrabc]]
[[Category: Uvrabc]]
[[Category: Uvrc]]
[[Category: Uvrc]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 09:50:16 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 09:17:12 2008''

Revision as of 06:17, 29 July 2008

Image:2nrz.png

Template:STRUCTURE 2nrz

Crystal structure of the C-terminal half of UvrC bound to its catalytic divalent cation

Template:ABSTRACT PUBMED 17245438

About this Structure

2NRZ 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 Tue Jul 29 09:17:12 2008

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