6APK

Trans-acting transferase from Disorazole synthase solved by serial femtosecond XFEL crystallography

6APK の概要

• エントリーDOI: 10.2210/pdb6apk/pdb
• 分子名称: DisD protein (2 entities in total)
• 機能のキーワード: transferase, disorazole synthase, xfel crystal structure, serial femtosecond crystallography
• 由来する生物種: Sorangium cellulosum
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 30663.04

構造登録者

Lyubimov, A.Y.,Mathews, I.I.,Uervivojnangkoorn, M.,Khosla, C.,Soltis, S.M.,Cohen, A.E. (登録日: 2017-08-17, 公開日: 2018-04-04, 最終更新日: 2023-10-04)

主引用文献

Mathews, I.I.,Allison, K.,Robbins, T.,Lyubimov, A.Y.,Uervirojnangkoorn, M.,Brunger, A.T.,Khosla, C.,DeMirci, H.,McPhillips, S.E.,Hollenbeck, M.,Soltis, M.,Cohen, A.E.
The Conformational Flexibility of the Acyltransferase from the Disorazole Polyketide Synthase Is Revealed by an X-ray Free-Electron Laser Using a Room-Temperature Sample Delivery Method for Serial Crystallography.
Biochemistry, 56:4751-4756, 2017

PubMed Abstract: The crystal structure of the trans-acyltransferase (AT) from the disorazole polyketide synthase (PKS) was determined at room temperature to a resolution of 2.5 Å using a new method for the direct delivery of the sample into an X-ray free-electron laser. A novel sample extractor efficiently delivered limited quantities of microcrystals directly from the native crystallization solution into the X-ray beam at room temperature. The AT structure revealed important catalytic features of this core PKS enzyme, including the occurrence of conformational changes around the active site. The implications of these conformational changes for polyketide synthase reaction dynamics are discussed.

PubMed: 28832129
DOI: 10.1021/acs.biochem.7b00711

実験手法

X-RAY DIFFRACTION (2.5 Å)