1lqm
From Proteopedia
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| - | + | {{STRUCTURE_1lqm| PDB=1lqm | SCENE= }} | |
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'''ESCHERICHIA COLI URACIL-DNA GLYCOSYLASE COMPLEX WITH URACIL-DNA GLYCOSYLASE INHIBITOR PROTEIN''' | '''ESCHERICHIA COLI URACIL-DNA GLYCOSYLASE COMPLEX WITH URACIL-DNA GLYCOSYLASE INHIBITOR PROTEIN''' | ||
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[[Category: Varshney, U.]] | [[Category: Varshney, U.]] | ||
[[Category: Vijayan, M.]] | [[Category: Vijayan, M.]] | ||
| - | [[Category: | + | [[Category: Base excision]] |
| - | [[Category: | + | [[Category: Dna repair]] |
| - | + | [[Category: Glycosylase]] | |
| - | [[Category: | + | [[Category: Inhibitor]] |
| - | [[Category: | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 00:11:08 2008'' |
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| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 21:11, 2 May 2008
ESCHERICHIA COLI URACIL-DNA GLYCOSYLASE COMPLEX WITH URACIL-DNA GLYCOSYLASE INHIBITOR PROTEIN
Overview
The structures of a new crystal form of free Escherichia coli uracil DNA glycosylase (UDG), containing four molecules in the asymmetric unit, and two forms of its complex with the proteinaceous inhibitor Ugi, containing two and four crystallographically independent complexes, have been determined. A comparison of these structures and the already known crystal structures containing UDG shows that the enzyme can be considered to be made up of two independently moving structural entities or domains. A detailed study of free and DNA-bound human enzyme strengthens this conclusion. The domains close upon binding to uracil-containing DNA, whereas they do not appear to do so upon binding to Ugi. The comparative study also shows that the mobility of the molecule involves the rigid-body movement of the domains superposed on flexibility within domains.
About this Structure
1LQM is a Protein complex structure of sequences from Bacillus phage pbs2 and Escherichia coli. Full crystallographic information is available from OCA.
Reference
Domain closure and action of uracil DNA glycosylase (UDG): structures of new crystal forms containing the Escherichia coli enzyme and a comparative study of the known structures involving UDG., Saikrishnan K, Bidya Sagar M, Ravishankar R, Roy S, Purnapatre K, Handa P, Varshney U, Vijayan M, Acta Crystallogr D Biol Crystallogr. 2002 Aug;58(Pt 8):1269-76. Epub 2002, Jul 20. PMID:12136137 Page seeded by OCA on Sat May 3 00:11:08 2008
