2QO3

Crystal Structure of [KS3][AT3] didomain from module 3 of 6-deoxyerthronolide B synthase

2QO3 の概要

• エントリーDOI: 10.2210/pdb2qo3/pdb
• 関連するPDBエントリー: 2HG4
• 分子名称: EryAII Erythromycin polyketide synthase modules 3 and 4, ACETATE ION, CHLORIDE ION, ... (5 entities in total)
• 機能のキーワード: ketosynthase, acyltransferase, phosphopantetheine, transferase
• 由来する生物種: Saccharopolyspora erythraea
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 194017.92

構造登録者

Khosla, C.,Cane, E.D.,Tang, Y.,Chen, Y.A.,Kim, C.Y. (登録日: 2007-07-19, 公開日: 2007-09-04, 最終更新日: 2024-11-06)

主引用文献

Tang, Y.,Chen, Y.A.,Kim, C.Y.,Cane, E.D.,Khosla, C.
Structural and mechanistic analysis of protein interactions in module 3 of the 6-deoxyerythronolide B synthase
Chem.Biol., 14:931-943, 2007

PubMed Abstract: We report the 2.6 A X-ray crystal structure of a 190 kDa homodimeric fragment from module 3 of the 6-deoxyerthronolide B synthase covalently bound to the inhibitor cerulenin. The structure shows two well-organized interdomain linker regions in addition to the full-length ketosynthase (KS) and acyltransferase (AT) domains. Analysis of the substrate-binding site of the KS domain suggests that a loop region at the homodimer interface influences KS substrate specificity. We also describe a model for the interaction of the catalytic domains with the acyl carrier protein (ACP) domain. The ACP is proposed to dock within a deep cleft between the KS and AT domains, with interactions that span both the KS homodimer and AT domain. In conjunction with other recent data, our results provide atomic resolution pictures of several catalytically relevant protein interactions in this remarkable family of modular megasynthases.

PubMed: 17719492
DOI: 10.1016/j.chembiol.2007.07.012

実験手法

X-RAY DIFFRACTION (2.59 Å)