4NTE

Crystal structure of DepH

Summary for 4NTE

• Entry DOI: 10.2210/pdb4nte/pdb
• Related: 4NTC 4NTD
• Descriptor: DepH, FLAVIN-ADENINE DINUCLEOTIDE, SODIUM ION, ... (5 entities in total)
• Functional Keywords: disulfide bond, natural sulfur products, romidepsin, oxidoreductase
• Biological source: Chromobacterium violaceum
• Total number of polymer chains: 2
• Total formula weight: 73687.57

Authors

Scharf, D.H.,Groll, M.,Habel, A.,Heinekamp, T.,Hertweck, C.,Brakhage, A.A.,Huber, E.M. (deposition date: 2013-12-02, release date: 2014-03-05, Last modification date: 2023-11-08)

Primary citation

Scharf, D.H.,Groll, M.,Habel, A.,Heinekamp, T.,Hertweck, C.,Brakhage, A.A.,Huber, E.M.
Flavoenzyme-Catalyzed Formation of Disulfide Bonds in Natural Products
Angew.Chem.Int.Ed.Engl., 53:2221-2224, 2014

PubMed Abstract: Nature provides a rich source of compounds with diverse chemical structures and biological activities, among them, sulfur-containing metabolites from bacteria and fungi. Some of these compounds bear a disulfide moiety that is indispensable for their bioactivity. Specialized oxidoreductases such as GliT, HlmI, and DepH catalyze the formation of this disulfide bridge in the virulence factor gliotoxin, the antibiotic holomycin, and the anticancer drug romidepsin, respectively. We have examined all three enzymes by X-ray crystallography and activity assays. Despite their differently sized substrate binding clefts and hence, their diverse substrate preferences, a unifying reaction mechanism is proposed based on the obtained crystal structures and further supported by mutagenesis experiments.

PubMed: 24446392
DOI: 10.1002/anie.201309302

Experimental method

X-RAY DIFFRACTION (1.9 Å)