PDBsum entry 2vpa

Oxidoreductase

PDB id: 2vpa

Contents

Protein chain

204 a.a. *

Ligands

ACT

PYR

Waters ×406

* Residue conservation analysis

PDB id:

2vpa

Name:

Oxidoreductase

Title:

High resolution crystal structure of the antibiotic resistance protein nima from deinococcus radiodurans

Structure:

Nima-related protein. Chain: a. Synonym: 5-nitroimidazole reductase. Engineered: yes. Other_details: includes the first 10 residues of the 21 residue long n-terminal his tag

Source:

Deinococcus radiodurans. Organism_taxid: 1299. Expressed in: escherichia coli. Expression_system_taxid: 469008.

Resolution:

1.20Å R-factor: 0.142 R-free: 0.180

Authors:

H.-K.S.Leiros,C.Tedesco,S.M.Mcsweeney

Key ref:

H.K.Leiros et al. (2008). High-resolution structure of the antibiotic resistance protein NimA from Deinococcus radiodurans. Acta Crystallogr Sect F Struct Biol Cryst Commun, 64, 442-447. PubMed id: 18540048

Date:

27-Feb-08 Release date: 19-Aug-08

Protein chain

Q9RW27  (Q9RW27_DEIRA) -  NimA-related protein from Deinococcus radiodurans (strain ATCC 13939 / DSM 20539 / JCM 16871 / CCUG 27074 / LMG 4051 / NBRC 15346 / NCIMB 9279 / VKM B-1422 / R1)

Seq: 195 a.a.

Struc: 204 a.a.*

* PDB and UniProt seqs differ at 1 residue position (black cross)

Acta Crystallogr Sect F Struct Biol Cryst Commun 64:442-447 (2008)

PubMed id: 18540048

High-resolution structure of the antibiotic resistance protein NimA from Deinococcus radiodurans.

H.K.Leiros, C.Tedesco, S.M.McSweeney.

ABSTRACT

Many anaerobic human pathogenic bacteria are treated using 5-nitroimidazole-based (5-Ni) antibiotics, a class of inactive prodrugs that contain a nitro group. The nitro group must be activated in an anaerobic one-electron reduction and is therefore dependent on the redox system in the target cells. Antibiotic resistance towards 5-Ni drugs is found to be related to the nim genes (nimA, nimB, nimC, nimD, nimE and nimF), which are proposed to encode a reductase that is responsible for converting the nitro group of the antibiotic into a nonbactericidal amine. A mechanism for the Nim enzyme has been proposed in which two-electron reduction of the nitro group leads to the generation of nontoxic derivatives and confers resistance against these antibiotics. The cofactor was found to be important in the mechanism and was found to be covalently linked to the reactive His71. In this paper, the 1.2 A atomic resolution crystal structure of the 5-nitroimidazole antibiotic resistance protein NimA from Deinococcus radiodurans (DrNimA) is presented. A planar cofactor is clearly visible and well defined in the electron-density map adjacent to His71, the identification of the cofactor and its properties are discussed.