2boo: Difference between revisions

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Bots, Bureaucrats, journal, Administrators
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[[Image:2boo.gif|left|200px]]
{{Seed}}
[[Image:2boo.png|left|200px]]


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{{STRUCTURE_2boo|  PDB=2boo  |  SCENE=  }}  
{{STRUCTURE_2boo|  PDB=2boo  |  SCENE=  }}  


'''THE CRYSTAL STRUCTURE OF URACIL-DNA N-GLYCOSYLASE (UNG) FROM DEINOCOCCUS RADIODURANS.'''
===THE CRYSTAL STRUCTURE OF URACIL-DNA N-GLYCOSYLASE (UNG) FROM DEINOCOCCUS RADIODURANS.===




==Overview==
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Uracil-DNA glycosylases are DNA-repair enzymes that catalyse the removal of promutagenic uracil from single- and double-stranded DNA, thereby initiating the base-excision repair (BER) pathway. Uracil in DNA can occur by mis-incorporation of dUMP in place of dTMP during DNA synthesis or by deamination of cytosine, resulting in U-A or U-G mispairs. The radiation-resistant bacterium Deinococcus radiodurans has an elevated number of uracil-DNA glycosylases compared with most other organisms. The crystal structure of dr0689 (uracil-DNA N-glycosylase), which has been shown to be the major contributor to the removal of mis-incorporated uracil bases in crude cell extracts of D. radiodurans, is reported.
The line below this paragraph, {{ABSTRACT_PUBMED_16041069}}, adds the Publication Abstract to the page
(as it appears on PubMed at http://www.pubmed.gov), where 16041069 is the PubMed ID number.
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{{ABSTRACT_PUBMED_16041069}}


==About this Structure==
==About this Structure==
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[[Category: Ung]]
[[Category: Ung]]
[[Category: Uracil-dna glycosylase]]
[[Category: Uracil-dna glycosylase]]
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