2JHQ

Crystal structure of Uracil DNA-glycosylase from Vibrio cholerae

Summary for 2JHQ

• Entry DOI: 10.2210/pdb2jhq/pdb
• Descriptor: URACIL DNA-GLYCOSYLASE, CHLORIDE ION (3 entities in total)
• Functional Keywords: mutational analysis, psychrophilic enzymes, ung, hydrolase, uracil-dna n-glycosylase, cold adaptation, vibrio salmonicida, dna damage, dna repair, glycosidase
• Biological source: VIBRIO CHOLERAE
• Cellular location: Cytoplasm (By similarity): Q9KPK8
• Total number of polymer chains: 1
• Total formula weight: 25511.32

Authors

Raeder, I.L.U.,Moe, E.,Willassen, N.P.,Smalas, A.O.,Leiros, I. (deposition date: 2007-02-23, release date: 2008-06-03, Last modification date: 2023-12-13)

Primary citation

Raeder, I.L.U.,Moe, E.,Willassen, N.P.,Smalas, A.O.,Leiros, I.
Structure of Uracil-DNA N-Glycosylase (Ung) from Vibrio Cholerae. Mapping Temperature Adaptation Through Structural and Mutational Analysis.
Acta Crystallogr.,Sect.F, 66:130-, 2010

PubMed Abstract: The crystal structure of Vibrio cholerae uracil-DNA N-glycosylase (vcUNG) has been determined to 1.5 A resolution. Based on this structure, a homology model of Aliivibrio salmonicida uracil-DNA N-glycosylase (asUNG) was built. A previous study demonstrated that asUNG possesses typical cold-adapted features compared with vcUNG, such as a higher catalytic efficiency owing to increased substrate affinity. Specific amino-acid substitutions in asUNG were suggested to be responsible for the increased substrate affinity and the elevated catalytic efficiency by increasing the positive surface charge in the DNA-binding region. The temperature adaptation of these enzymes has been investigated using structural and mutational analyses, in which mutations of vcUNG demonstrated an increased substrate affinity that more resembled that of asUNG. Visualization of surface potentials revealed a more positive potential for asUNG compared with vcUNG; a modelled double mutant of vcUNG had a potential around the substrate-binding region that was more like that of asUNG, thus rationalizing the results obtained from the kinetic studies.

PubMed: 20124707
DOI: 10.1107/S1744309109052063

Experimental method

X-RAY DIFFRACTION (1.5 Å)