7YP5

Crystal structure of elaiophylin glycosyltransferase in complex with TDP

7YP5 の概要

• エントリーDOI: 10.2210/pdb7yp5/pdb
• 分子名称: Glycosyltransferase, THYMIDINE-5'-DIPHOSPHATE, R-1,2-PROPANEDIOL, ... (5 entities in total)
• 機能のキーワード: glycosyltransferase, elaiophylin, gt1, transferase
• 由来する生物種: Streptomyces sp. SCSIO 01934
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 98614.60

構造登録者

Xu, T.,Liu, Q.,Gan, Q.,Liu, J. (登録日: 2022-08-02, 公開日: 2022-11-02, 最終更新日: 2023-11-29)

主引用文献

Xu, T.,Gan, Q.,Liu, Q.,Chen, R.,Zhen, X.,Zhang, C.,Liu, J.
Substrate-induced dimerization of elaiophylin glycosyltransferase reveals a novel self-activating form of glycosyltransferase for symmetric glycosylation.
Acta Crystallogr D Struct Biol, 78:1235-1248, 2022

PubMed Abstract: Elaiophylin (Ela), a unique 16-membered symmetric macrodiolide antibiotic, displays broad biological activity. Two rare 2-deoxy-L-fucose moieties at the ends of Ela are critical for its activity. Previously, elaiophylin glycosyltransferase (ElaGT) was identified as the enzyme that is responsible for the symmetric glycosylation of Ela, acting as a potential enzymatic tool for enhancing the diversity and activity of Ela. However, a symmetric catalytic mechanism has never been reported for a glycosyltransferase (GT). To explore the catalytic mechanism, the structure of ElaGT was determined in four forms: the apo form and Ela-bound, thymidine diphosphate-bound and uridine diphosphate-bound forms. In the Ela-bound structure, two ElaGTs form a `face-to-face' C2-symmetric homodimer with a continuous acceptor-binding pocket, allowing a molecule of Ela to shuffle through. Interestingly, this dimer interface resembles that of the activator-dependent GT EryCIII with its activator EryCII. Sequence analysis also indicates that ElaGT belongs to the activator-dependent GT family, but no putative activator has been identified in the Ela gene cluster. It was then found that the ElaGT homodimer may utilize this `face-to-face' arrangement to stabilize the Ela-binding loops on the interface and to simultaneously allosterically regulate the catalytic center. Therefore, these structures present a novel self-activating model for symmetric sugar transfer in the GT family and a new potential regulation site for substrate specificity.

PubMed: 36189743
DOI: 10.1107/S2059798322008658

実験手法

X-RAY DIFFRACTION (2.33 Å)