1LQM
ESCHERICHIA COLI URACIL-DNA GLYCOSYLASE COMPLEX WITH URACIL-DNA GLYCOSYLASE INHIBITOR PROTEIN
Summary for 1LQM
Entry DOI | 10.2210/pdb1lqm/pdb |
Related | 1EUI 1LQG 1LQJ |
Descriptor | URACIL-DNA GLYCOSYLASE, URACIL-DNA GLYCOSYLASE INHIBITOR (3 entities in total) |
Functional Keywords | glycosylase, inhibitor, dna repair, base excision, complex (hydrolase-inhibitor), hydrolase-hydrolase inhibitor complex, hydrolase/hydrolase inhibitor |
Biological source | Escherichia coli More |
Cellular location | Cytoplasm: P12295 |
Total number of polymer chains | 8 |
Total formula weight | 140831.42 |
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 citation | Saikrishnan, 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: 12136137DOI: 10.1107/S0907444902009599 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (3.2 Å) |
Structure validation
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