6R1E

Structure of dodecin from Streptomyces coelicolor

6R1E の概要

• エントリーDOI: 10.2210/pdb6r1e/pdb
• 分子名称: dodecin, FLAVIN MONONUCLEOTIDE, COENZYME A, ... (7 entities in total)
• 機能のキーワード: flavin storage, dodecamer, protein complex, flavoprotein
• 由来する生物種: Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145)
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 37388.87

構造登録者

Essen, L.-O.,Sander, B. (登録日: 2019-03-14, 公開日: 2019-03-27, 最終更新日: 2024-01-31)

主引用文献

Bourdeaux, F.,Ludwig, P.,Paithankar, K.,Sander, B.,Essen, L.O.,Grininger, M.,Mack, M.
Comparative biochemical and structural analysis of the flavin-binding dodecins fromStreptomyces davaonensisandStreptomyces coelicolorreveals striking differences with regard to multimerization.
Microbiology (Reading, Engl.), 165:1095-1106, 2019

PubMed Abstract: Dodecins are small flavin-binding proteins that are widespread amongst haloarchaeal and bacterial species. Haloarchaeal dodecins predominantly bind riboflavin, while bacterial dodecins have been reported to bind riboflavin-5'-phosphate, also called flavin mononucleotide (FMN), and the FMN derivative, flavin adenine dinucleotide (FAD). Dodecins form dodecameric complexes and represent buffer systems for cytoplasmic flavins. In this study, dodecins of the bacteria (SdDod) and (ScDod) were investigated. Both dodecins showed an unprecedented low affinity for riboflavin, FMN and FAD when compared to other bacterial dodecins. Significant binding of FMN and FAD occurred at relatively low temperatures and under acidic conditions. X-ray diffraction analyses of SdDod and ScDod revealed that the structures of both dodecins are highly similar, which explains their similar binding properties for FMN and FAD. In contrast, SdDod and ScDod showed very different properties with regard to the stability of their dodecameric complexes. Site-directed mutagenesis experiments revealed that a specific salt bridge (D10-K62) is responsible for this difference in stability.

PubMed: 31339487
DOI: 10.1099/mic.0.000835

実験手法

X-RAY DIFFRACTION (2.6 Å)