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Title | Mapping the catalytic conformations of an assembly-line polyketide synthase module. |
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Journal, issue, pages | Science, Vol. 374, Issue 6568, Page 729-734, Year 2021 |
Publish date | Nov 5, 2021 |
![]() | Dillon P Cogan / Kaiming Zhang / Xiuyuan Li / Shanshan Li / Grigore D Pintilie / Soung-Hun Roh / Charles S Craik / Wah Chiu / Chaitan Khosla / ![]() ![]() ![]() |
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 ...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. |
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Methods | EM (single particle) |
Resolution | 3.2 - 4.3 Å |
Structure data | EMDB-23710, PDB-7m7e: EMDB-23711, PDB-7m7f: EMDB-23712, PDB-7m7g: EMDB-23713, PDB-7m7h: EMDB-23714, PDB-7m7i: EMDB-23715, PDB-7m7j: |
Chemicals | ![]() ChemComp-PN7: |
Source |
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