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1odg

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[[Image:1odg.gif|left|200px]]
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{{Seed}}
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[[Image:1odg.png|left|200px]]
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{{STRUCTURE_1odg| PDB=1odg | SCENE= }}
{{STRUCTURE_1odg| PDB=1odg | SCENE= }}
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'''VERY-SHORT-PATCH DNA REPAIR ENDONUCLEASE BOUND TO ITS REACTION PRODUCT SITE'''
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===VERY-SHORT-PATCH DNA REPAIR ENDONUCLEASE BOUND TO ITS REACTION PRODUCT SITE===
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==Overview==
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Very-short-patch repair (Vsr) enzymes occur in a variety of bacteria, where they initiate nucleotide excision repair of G:T mismatches arising by deamination of 5-methyl-cytosines in specific regulatory sequences. We have now determined the structure of the archetypal dcm-Vsr endonuclease from Escherichia coli bound to the cleaved authentic hemi-deaminated/hemi-methylated dcm sequence 5'-C-OH-3' 5'-p-T-p-A-p-G-p-G-3'/3'-G-p-G-p-T-p(Me5)C-p-C formed by self-assembly of a 12mer oligonucleotide into a continuous nicked DNA superhelix. The structure reveals the presence of a Hoogsteen base pair within the deaminated recognition sequence and the substantial distortions of the DNA that accompany Vsr binding to product sites.
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The line below this paragraph, {{ABSTRACT_PUBMED_12626704}}, adds the Publication Abstract to the page
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(as it appears on PubMed at http://www.pubmed.gov), where 12626704 is the PubMed ID number.
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{{ABSTRACT_PUBMED_12626704}}
==About this Structure==
==About this Structure==
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[[Category: Very short patch repair]]
[[Category: Very short patch repair]]
[[Category: Zinc]]
[[Category: Zinc]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 03:42:19 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 17:40:14 2008''

Revision as of 14:40, 28 July 2008

Image:1odg.png

Template:STRUCTURE 1odg

VERY-SHORT-PATCH DNA REPAIR ENDONUCLEASE BOUND TO ITS REACTION PRODUCT SITE

Template:ABSTRACT PUBMED 12626704

About this Structure

1ODG is a Protein complex structure of sequences from Escherichia coli. Full crystallographic information is available from OCA.

Reference

Crystal structure of the Escherichia coli dcm very-short-patch DNA repair endonuclease bound to its reaction product-site in a DNA superhelix., Bunting KA, Roe SM, Headley A, Brown T, Savva R, Pearl LH, Nucleic Acids Res. 2003 Mar 15;31(6):1633-9. PMID:12626704

Page seeded by OCA on Mon Jul 28 17:40:14 2008

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