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 and Sagar, Bidya M and Ravishankar, R and Roy, S and Purnapatre, K and Handa, P and Varshney, U and 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. In: Acta Crystallographica Section D: Biological Crystallography, 58 (8). pp. 1269-1276.

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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:	Journal Article
Publication:	Acta Crystallographica Section D: Biological Crystallography
Publisher:	International Union of Crystallography
Additional Information:	The copyright for this article belongs to International Union of Crystallography.
Keywords:	uracil dna;glycosylase;UDG;escherichia coli;enzyme
Department/Centre:	Division of Biological Sciences > Molecular Biophysics Unit Division of Biological Sciences > Microbiology & Cell Biology
Date Deposited:	25 Oct 2004
Last Modified:	19 Sep 2010 04:16
URI:	http://eprints.iisc.ac.in/id/eprint/2100

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