7M7E

6-Deoxyerythronolide B synthase (DEBS) hybrid module (M3/1) in complex with antibody fragment 1B2

7M7E の概要

• エントリーDOI: 10.2210/pdb7m7e/pdb
• EMDBエントリー: 23710 23711 23712 23713 23714 23715
• 分子名称: 6-deoxyerythronolide-B synthase EryA2, modules 3 and 4,EryAI,6-deoxyerythronolide-B synthase EryA3, modules 5 and 6 chimera, 1B2 (heavy chain), 1B2 (light chain) (3 entities in total)
• 機能のキーワード: polyketide synthase, antibody fragment, biosynthetic protein-immune system complex, biosynthetic protein/immune system
• 由来する生物種: Saccharopolyspora erythraea (Streptomyces erythraeus); 詳細
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 427834.29

構造登録者

Cogan, D.P.,Zhang, K.,Chiu, W.,Khosla, C. (登録日: 2021-03-28, 公開日: 2021-11-17, 最終更新日: 2025-05-14)

主引用文献

Cogan, D.P.,Zhang, K.,Li, X.,Li, S.,Pintilie, G.D.,Roh, S.H.,Craik, C.S.,Chiu, W.,Khosla, C.
Mapping the catalytic conformations of an assembly-line polyketide synthase module.
Science, 374:729-734, 2021

PubMed Abstract: Assembly-line polyketide synthases, such as the 6-deoxyerythronolide B synthase (DEBS), are large enzyme factories prized for their ability to produce specific and complex polyketide products. By channeling protein-tethered substrates across multiple active sites in a defined linear sequence, these enzymes facilitate programmed small-molecule syntheses that could theoretically be harnessed to access countless polyketide product structures. Using cryogenic electron microscopy to study DEBS module 1, we present a structural model describing this substrate-channeling phenomenon. Our 3.2- to 4.3-angstrom-resolution structures of the intact module reveal key domain-domain interfaces and highlight an unexpected module asymmetry. We also present the structure of a product-bound module that shines light on a recently described “turnstile” mechanism for transient gating of active sites along the assembly line.

PubMed: 34735239
DOI: 10.1126/science.abi8358

実験手法

ELECTRON MICROSCOPY (3.2 Å)