4NTC
Crystal structure of GliT
4NTC の概要
エントリーDOI | 10.2210/pdb4ntc/pdb |
関連するPDBエントリー | 3FBS 4NTD 4NTE |
分子名称 | GliT, FLAVIN-ADENINE DINUCLEOTIDE (3 entities in total) |
機能のキーワード | disulfide bond, epipolythiodioxopiperazine, gliotoxin, natural sulfur products, oxidoreductase |
由来する生物種 | Aspergillus fumigatus |
タンパク質・核酸の鎖数 | 2 |
化学式量合計 | 73824.50 |
構造登録者 | Scharf, D.H.,Groll, M.,Habel, A.,Heinekamp, T.,Hertweck, C.,Brakhage, A.A.,Huber, E.M. (登録日: 2013-12-02, 公開日: 2014-03-05, 最終更新日: 2024-11-06) |
主引用文献 | 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 Cited by 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: 24446392DOI: 10.1002/anie.201309302 主引用文献が同じPDBエントリー |
実験手法 | X-RAY DIFFRACTION (1.9 Å) |
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