EMD-23710

Single-particle
3.2 Å
EMD-23710 Deposition: 28/03/2021
Map released: 17/11/2021
Last modified: 30/10/2024
Overview 3D View Sample Experiment Validation Volume Browser Additional data Links
Overview 3D View Sample Experiment Validation Volume Browser Additional data Links

EMD-23710

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

EMD-23710

Single-particle
3.2 Å
EMD-23710 Deposition: 28/03/2021
Map released: 17/11/2021
Last modified: 30/10/2024
Overview 3D View Sample Experiment Validation Volume Browser Additional data Links
Sample Organism: Saccharopolyspora erythraea, Homo sapiens
Sample: Complex between DEBS M3/1TE and antibody fragment 1B2
Fitted models: 7m7e (Avg. Q-score: 0.449)

Deposition Authors: Cogan DP , Zhang K
Mapping the catalytic conformations of an assembly-line polyketide synthase module.
Cogan DP , Zhang K , Li X , Li S , Pintilie GD , Roh SH , Craik CS , Chiu W , Khosla C
(2021) Science , 374 , 729 - 734
PUBMED: 34735239
DOI: doi:10.1126/science.abi8358
ISSN: 1095-9203
ASTM: SCIEAS
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.