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| - | [[Image:2owq.jpg|left|200px]] | + | {{Seed}} |
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| | {{STRUCTURE_2owq| PDB=2owq | SCENE= }} | | {{STRUCTURE_2owq| PDB=2owq | SCENE= }} |
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| - | '''Crystal structure of vaccinia virus uracil-DNA glycosylase'''
| + | ===Crystal structure of vaccinia virus uracil-DNA glycosylase=== |
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| - | ==Overview==
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| - | 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.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_17605817}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 17605817 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_17605817}} |
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| | ==About this Structure== | | ==About this Structure== |
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| | [[Category: And parallel beta-sheet of 4 strands in the order 2134]] | | [[Category: And parallel beta-sheet of 4 strands in the order 2134]] |
| | [[Category: Novel features: beta-sheets at n- and c-terminus]] | | [[Category: Novel features: beta-sheets at n- and c-terminus]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 11:49:27 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 18:24:46 2008'' |
Revision as of 15:24, 27 July 2008
Template:STRUCTURE 2owq
Crystal structure of vaccinia virus uracil-DNA glycosylase
Template:ABSTRACT PUBMED 17605817
About this Structure
2OWQ is a Single protein structure of sequence from Vaccinia virus. Full crystallographic information is available from OCA.
Reference
Crystal structure of vaccinia virus uracil-DNA glycosylase reveals dimeric assembly., Schormann N, Grigorian A, Samal A, Krishnan R, DeLucas L, Chattopadhyay D, BMC Struct Biol. 2007 Jul 2;7:45. PMID:17605817
Page seeded by OCA on Sun Jul 27 18:24:46 2008
