PDBsum entry 2jhq

Hydrolase

PDB id: 2jhq

Contents

Protein chain

223 a.a. *

Metals

_CL

Waters ×327

* Residue conservation analysis

PDB id:

2jhq

Name:

Hydrolase

Title:

Crystal structure of uracil DNA-glycosylase from vibrio cholerae

Structure:

Uracil DNA-glycosylase. Chain: a. Synonym: udg. Engineered: yes

Source:

Vibrio cholerae. Organism_taxid: 666. Atcc: 14035. Expressed in: escherichia coli. Expression_system_taxid: 511693.

Resolution:

1.50Å R-factor: 0.177 R-free: 0.210

Authors:

I.L.U.Raeder,E.Moe,N.P.Willassen,A.O.Smalas,I.Leiros

Key ref:

I.L.Raeder et al. (2010). Structure of uracil-DNA N-glycosylase (UNG) from Vibrio cholerae: mapping temperature adaptation through structural and mutational analysis. Acta Crystallogr Sect F Struct Biol Cryst Commun, 66, 130-136. PubMed id: 20124707

Date:

23-Feb-07 Release date: 03-Jun-08

Protein chain

Q9KPK8  (UNG_VIBCH) -  Uracil-DNA glycosylase from Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961)

Seq: 226 a.a.

Struc: 223 a.a.

Enzyme reactions

• Enzyme class: E.C.3.2.2.27 - uracil-DNA glycosylase.

Acta Crystallogr Sect F Struct Biol Cryst Commun 66:130-136 (2010)

PubMed id: 20124707

Structure of uracil-DNA N-glycosylase (UNG) from Vibrio cholerae: mapping temperature adaptation through structural and mutational analysis.

I.L.Raeder, E.Moe, N.P.Willassen, A.O.Smalås, I.Leiros.

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.