2WQF

Crystal Structure of the Nitroreductase CinD from Lactococcus lactis in Complex with FMN

Summary for 2WQF

• Entry DOI: 10.2210/pdb2wqf/pdb
• Descriptor: COPPER INDUCED NITROREDUCTASE D, FLAVIN MONONUCLEOTIDE (3 entities in total)
• Functional Keywords: nitroreductase, copr regulated protein, oxidoreductase
• Biological source: LACTOCOCCUS LACTIS
• Total number of polymer chains: 1
• Total formula weight: 23018.76

Authors

Waltersperger, S.M.,Oberholzer, A.E.,Solioz, M.,Baumann, U. (deposition date: 2009-08-20, release date: 2010-06-30, Last modification date: 2023-12-20)

Primary citation

Mermod, M.,Mourlane, F.,Waltersperger, S.,Oberholzer, A.E.,Baumann, U.,Solioz, M.
Structure and Function of Cind (Ytjd) of Lactococcus Lactis, a Copper-Induced Nitroreductase Involved in Defense Against Oxidative Stress.
J.Bacteriol., 192:4172-, 2010

PubMed Abstract: In Lactococcus lactis IL1403, 14 genes are under the control of the copper-inducible CopR repressor. This so-called CopR regulon encompasses the CopR regulator, two putative CPx-type copper ATPases, a copper chaperone, and 10 additional genes of unknown function. We addressed here the function of one of these genes, ytjD, which we renamed cinD (copper-induced nitroreductase). Copper, cadmium, and silver induced cinD in vivo, as shown by real-time quantitative PCR. A knockout mutant of cinD was more sensitive to oxidative stress exerted by 4-nitroquinoline-N-oxide and copper. Purified CinD is a flavoprotein and reduced 2,6-dichlorophenolindophenol and 4-nitroquinoline-N-oxide with k(cat) values of 27 and 11 s(-1), respectively, using NADH as a reductant. CinD also exhibited significant catalase activity in vitro. The X-ray structure of CinD was resolved at 1.35 A and resembles those of other nitroreductases. CinD is thus a nitroreductase which can protect L. lactis against oxidative stress that could be exerted by nitroaromatic compounds and copper.

PubMed: 20562311
DOI: 10.1128/JB.00372-10

Experimental method

X-RAY DIFFRACTION (1.35 Å)