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1LQM

ESCHERICHIA COLI URACIL-DNA GLYCOSYLASE COMPLEX WITH URACIL-DNA GLYCOSYLASE INHIBITOR PROTEIN

Summary for 1LQM
Entry DOI10.2210/pdb1lqm/pdb
Related1EUI 1LQG 1LQJ
DescriptorURACIL-DNA GLYCOSYLASE, URACIL-DNA GLYCOSYLASE INHIBITOR (3 entities in total)
Functional Keywordsglycosylase, inhibitor, dna repair, base excision, complex (hydrolase-inhibitor), hydrolase-hydrolase inhibitor complex, hydrolase/hydrolase inhibitor
Biological sourceEscherichia coli
More
Cellular locationCytoplasm: P12295
Total number of polymer chains8
Total formula weight140831.42
Authors
Saikrishnan, K.,Sagar, M.B.,Ravishankar, R.,Roy, S.,Purnapatre, K.,Varshney, U.,Vijayan, M. (deposition date: 2002-05-10, release date: 2002-11-10, Last modification date: 2024-02-14)
Primary citationSaikrishnan, K.,Bidya Sagar, M.,Ravishankar, R.,Roy, S.,Purnapatre, K.,Handa, P.,Varshney, U.,Vijayan, M.
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 Crystallogr.,Sect.D, 58:1269-1276, 2002
Cited by
PubMed 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.
PubMed: 12136137
DOI: 10.1107/S0907444902009599
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (3.2 Å)
Structure validation

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