PDBsum entry 2boo

Hydrolase

PDB id

2boo

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Contents

			Protein chain

					230 a.a. *

			Ligands

					NO3 ×3

			Waters ×154

* Residue conservation analysis

PDB id:

2boo

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Name:

Hydrolase

Title:

The crystal structure of uracil-DNA n-glycosylase (ung) from deinococcus radiodurans.

Structure:

Uracil-DNA glycosylase. Chain: a. Synonym: udg. Engineered: yes. Other_details: residues 1-16 and 247 not visible in electron density

Source:

Deinococcus radiodurans. Organism_taxid: 243230. Strain: r1. Expressed in: escherichia coli. Expression_system_taxid: 469008.

Resolution:

1.80Å

R-factor:

0.236

R-free:

0.272

Authors:

I.Leiros,E.Moe,A.O.Smalas,S.Mcsweeney

Key ref:

I.Leiros et al. (2005). Structure of the uracil-DNA N-glycosylase (UNG) from Deinococcus radiodurans. Acta Crystallogr D Biol Crystallogr, 61, 1049-1056. PubMed id: 16041069 DOI: 10.1107/S090744490501382X

Date:

13-Apr-05

Release date:

27-Jul-05

PROCHECK

	Headers

	References

Protein chain

Q9RWH9 (UNG_DEIRA) - Uracil-DNA glycosylase from Deinococcus radiodurans (strain ATCC 13939 / DSM 20539 / JCM 16871 / CCUG 27074 / LMG 4051 / NBRC 15346 / NCIMB 9279 / VKM B-1422 / R1)

Seq: Struc:					247 a.a. 230 a.a.

Key:

PfamA domain

Secondary structure

CATH domain



		Enzyme reactions

Enzyme class:

E.C.3.2.2.27 - uracil-DNA glycosylase.

[IntEnz] [ExPASy] [KEGG] [BRENDA]

DOI no: 10.1107/S090744490501382X	Acta Crystallogr D Biol Crystallogr 61:1049-1056 (2005)
PubMed id: 16041069

Structure of the uracil-DNA N-glycosylase (UNG) from Deinococcus radiodurans.
I.Leiros, E.Moe, A.O.Smalås, S.McSweeney.

ABSTRACT

Uracil-DNA glycosylases are DNA-repair enzymes that catalyse the removal of promutagenic uracil from single- and double-stranded DNA, thereby initiating the base-excision repair (BER) pathway. Uracil in DNA can occur by mis-incorporation of dUMP in place of dTMP during DNA synthesis or by deamination of cytosine, resulting in U-A or U-G mispairs. The radiation-resistant bacterium Deinococcus radiodurans has an elevated number of uracil-DNA glycosylases compared with most other organisms. The crystal structure of dr0689 (uracil-DNA N-glycosylase), which has been shown to be the major contributor to the removal of mis-incorporated uracil bases in crude cell extracts of D. radiodurans, is reported.

Selected figure(s)



	Figure 2. Figure 2 Ribbon illustration of the crystal structure of drUNG. The nitrate molecules are shown as ball-and-stick representations in atom colour, with the one bound in the active site labelled in bold.		Figure 5. Figure 5

Figures were selected by an automated process.

Literature references that cite this PDB file's key reference

PubMed id

Reference

18540048

H.K.Leiros, C.Tedesco, and S.M.McSweeney (2008).
High-resolution structure of the antibiotic resistance protein NimA from Deinococcus radiodurans.

Acta Crystallogr Sect F Struct Biol Cryst Commun, 64, 442-447.

PDB code:

2vpa

16223719

E.Moe, I.Leiros, A.O.Smalås, and S.McSweeney (2006).
The crystal structure of mismatch-specific uracil-DNA glycosylase (MUG) from Deinococcus radiodurans reveals a novel catalytic residue and broad substrate specificity.

J Biol Chem, 281, 569-577.

PDB codes:

2c2p 2c2q

17142904

P.Singh, R.K.Talawar, P.D.Krishna, U.Varshney, and M.Vijayan (2006).
Overexpression, purification, crystallization and preliminary X-ray analysis of uracil N-glycosylase from Mycobacterium tuberculosis in complex with a proteinaceous inhibitor.

Acta Crystallogr Sect F Struct Biol Cryst Commun, 62, 1231-1234.

The most recent references are shown first. Citation data come partly from CiteXplore and partly from an automated harvesting procedure. Note that this is likely to be only a partial list as not all journals are covered by either method. However, we are continually building up the citation data so more and more references will be included with time. Where a reference describes a PDB structure, the PDB code is shown on the right.