2VPA

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

Summary for 2VPA

• Entry DOI: 10.2210/pdb2vpa/pdb
• Related: 1W3O 1W3P 1W3Q 1W3R
• Descriptor: NIMA-RELATED PROTEIN, ACETATE ION, PYRUVIC ACID, ... (4 entities in total)
• Functional Keywords: cofactor, atomic resolution, oxidoreductase
• Biological source: DEINOCOCCUS RADIODURANS
• Total number of polymer chains: 1
• Total formula weight: 24614.34

Authors

Leiros, H.-K.S.,Tedesco, C.,McSweeney, S.M. (deposition date: 2008-02-27, release date: 2008-08-19, Last modification date: 2023-12-13)

Primary citation

Leiros, H.-K.S.,Tedesco, C.,Mcsweeney, S.M.
High-Resolution Structure of the Antibiotic Resistance Protein Nima from Deinococcus Radiodurans.
Acta Crystallogr.,Sect.F, 64:442-, 2008

PubMed 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.

PubMed: 18540048
DOI: 10.1107/S1744309108009901

Experimental method

X-RAY DIFFRACTION (1.2 Å)