3A7N

Crystal structure of uracil-DNA glycosylase from Mycobacterium tuberculosis

Summary for 3A7N

• Entry DOI: 10.2210/pdb3a7n/pdb
• Related: 2ZHX
• Descriptor: Uracil-DNA glycosylase, CITRATE ANION (3 entities in total)
• Functional Keywords: ung-ugi interactions, ung-dna complex, citrate as protein ligand, ligand binding, inhibitor design, dna damage, dna repair, glycosidase, hydrolase
• Biological source: Mycobacterium tuberculosis H37Rv
• Total number of polymer chains: 1
• Total formula weight: 26191.74

Authors

Kaushal, P.S.,Talawar, R.K.,Varshney, U.,Vijayan, M. (deposition date: 2009-09-29, release date: 2010-08-11, Last modification date: 2023-11-01)

Primary citation

Kaushal, P.S.,Talawar, R.K.,Varshney, U.,Vijayan, M.
Structure of uracil-DNA glycosylase from Mycobacterium tuberculosis: insights into interactions with ligands
Acta Crystallogr.,Sect.F, 66:887-892, 2010

PubMed Abstract: Uracil N-glycosylase (Ung) is the most thoroughly studied of the group of uracil DNA-glycosylase (UDG) enzymes that catalyse the first step in the uracil excision-repair pathway. The overall structure of the enzyme from Mycobacterium tuberculosis is essentially the same as that of the enzyme from other sources. However, differences exist in the N- and C-terminal stretches and some catalytic loops. Comparison with appropriate structures indicate that the two-domain enzyme closes slightly when binding to DNA, while it opens slightly when binding to the proteinaceous inhibitor Ugi. The structural changes in the catalytic loops on complexation reflect the special features of their structure in the mycobacterial protein. A comparative analysis of available sequences of the enzyme from different sources indicates high conservation of amino-acid residues in the catalytic loops. The uracil-binding pocket in the structure is occupied by a citrate ion. The interactions of the citrate ion with the protein mimic those of uracil, in addition to providing insights into other possible interactions that inhibitors could be involved in.

PubMed: 20693660
DOI: 10.1107/S1744309110023043

Experimental method

X-RAY DIFFRACTION (1.95 Å)