Saikrishnan, K. ; Bidya Sagar, M. ; Ravishankar, R. ; Roy, S. ; Purnapatre, K. ; Handa, P. ; Varshney, U. ; Vijayan, M. (2002) 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 Acta Crystallographica Section D, 58 . pp. 1269-1276. ISSN 0907-4449
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Official URL: http://scripts.iucr.org/cgi-bin/paper?be0014
Related URL: http://dx.doi.org/10.1107/S0907444902009599
Abstract
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.
Item Type: | Article |
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Source: | Copyright of this article belongs to International Union of Crystallography. |
Keywords: | Uracil DNA Glycosylase |
ID Code: | 53869 |
Deposited On: | 10 Aug 2011 09:34 |
Last Modified: | 18 May 2016 06:49 |
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