Crystal structure of vaccinia virus uracil-DNA glycosylase reveals dimeric assembly.

Crystal structure of vaccinia virus uracil-DNA glycosylase reveals dimeric assembly. Research Abstract Details 

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Crystal structure of vaccinia virus uracil-DNA glycosylase reveals dimeric assembly. Abstract Text:

Norbert Schormann,Alexei Grigorian,Alexandra Samal,Raman Krishnan,Lawrence DeLucas,Debasish Chattopadhyay,

BACKGROUND: Uracil-DNA glycosylases (UDGs) catalyze excision of uracil from DNA. Vaccinia virus, which is the prototype of poxviruses, encodes a UDG (vvUDG) that is significantly different from the UDGs of other organisms in primary, secondary and tertiary structure and characteristic motifs. It adopted a novel catalysis-independent role in DNA replication that involves interaction with a viral protein, A20, to form the processivity factor. UDG:A20 association is essential for assembling of the processive DNA polymerase complex. The structure of the protein must have provisions for such interactions with A20. This paper provides the first glimpse into the structure of a poxvirus UDG. RESULTS: Results of dynamic light scattering experiments and native size exclusion chromatography showed that vvUDG is a dimer in solution. The dimeric assembly is also maintained in two crystal forms. The core of vvUDG is reasonably well conserved but the structure contains one additional beta-sheet at each terminus. A glycerol molecule is found in the active site of the enzyme in both crystal forms. Interaction of this glycerol molecule with the protein possibly mimics the enzyme-substrate (uracil) interactions. CONCLUSION: The crystal structures reveal several distinctive features of vvUDG. The new structural features may have evolved for adopting novel functions in the replication machinery of poxviruses. The mode of interaction between the subunits in the dimers suggests a possible model for binding to its partner and the nature of the processivity factor in the polymerase complex.

Crystal structure of vaccinia virus uracil-DNA glycosylase reveals dimeric assembly. Publishing Authors By Initials

N Schormann,A Grigorian,A Samal,R Krishnan,L DeLucas,D Chattopadhyay,

For similar proteins: viral proteins research abstracts see: proteins: viral proteins research

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Crystal structure of vaccinia virus uracil-DNA glycosylase reveals dimeric assembly. Journal Published:

PUBLICATION TYPE: Research Support, Non-U.S. Gov

Journal: BMC structural biology

VOLUME: 7

Page Numbers: 45

Journal Abbreviation: BMC Struct. Biol.

ISSN: 1472-6807

DAY: 2

MONTH: 07

YEAR: 2007

Crystal structure of vaccinia virus uracil-DNA glycosylase reveals dimeric assembly. Information

Number of References:

LANGUAGE: eng

NlmUniqueID: 101088689

Crystal structure of vaccinia virus uracil-DNA glycosylase reveals dimeric assembly. Keywords Mesh Terms:

KEYWORDS: Viral Proteins

MESH TERMS: metabolism

Chemical & Substance for Abstract: Crystal structure of vaccinia virus uracil-DNA glycosylase reveals dimeric assembly. Information

Substance Name: Uracil-DNA Glycosidase

Registry Number: EC 3.2.2.-

Grant and Affiliation Information for Crystal structure of vaccinia virus uracil-DNA glycosylase reveals dimeric assembly.

AFFILIATION: Center for Biophysical Sciences & Engineering, University of Alabama at Birmingham, Birmingham, AL 35294, USA. nschorm@uab.edu <nschorm@uab.edu>

Country: England

AGENCY: United States NIAID

GRANT: U54 AI 057157

ACRONYM: AI

MEDLINETA: BMC Struct Biol

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