5COH

Crystal structure of a novel disulfide oxidoreductase from Deinococcus radiodurans crystallized in presence of beta-mercaptoethanol

Summary for 5COH

• Entry DOI: 10.2210/pdb5coh/pdb
• Related: 5cnw 5co3 5cp1
• Descriptor: FrnE protein (2 entities in total)
• Functional Keywords: disulfide oxidoreductase, disulfide isomerase, frne, oxidoreductase
• Biological source: Deinococcus radiodurans (strain ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB 9279 / R1 / VKM B-1422)
• Total number of polymer chains: 1
• Total formula weight: 28493.88

Authors

Bihani, S.C.,Panicker, L.,Kumar, V. (deposition date: 2015-07-20, release date: 2016-07-20, Last modification date: 2024-10-09)

Primary citation

Bihani, S.C.,Panicker, L.,Rajpurohit, Y.S.,Misra, H.S.,Kumar, V.
drFrnE Represents a Hitherto Unknown Class of Eubacterial Cytoplasmic Disulfide Oxido-Reductases.
Antioxid. Redox Signal., 28:296-310, 2018

PubMed Abstract: Living cells employ thioredoxin and glutaredoxin disulfide oxido-reductases to protect thiol groups in intracellular proteins. FrnE protein of Deinococcus radiodurans (drFrnE) is a disulfide oxido-reductase that is induced in response to Cd exposure and is involved in cadmium and radiation tolerance. The aim of this study is to probe structure, function, and cellular localization of FrnE class of proteins.

PubMed: 28899103
DOI: 10.1089/ars.2016.6960

Experimental method

X-RAY DIFFRACTION (1.801 Å)