Details

Autor(en) / Beteiligte

• Bagde, Saket R
• Mathews, Irimpan I
• Fromme, J Christopher
• Kim, Chu-Young

Titel

Modular polyketide synthase contains two reaction chambers that operate asynchronously

Ist Teil von

• Science (American Association for the Advancement of Science), 2021-11, Vol.374 (6568), p.723-729

Ort / Verlag

United States: The American Association for the Advancement of Science

Erscheinungsjahr

2021

Quelle

Science Online_科学在线

Beschreibungen/Notizen

• Type I modular polyketide synthases are homodimeric multidomain assembly line enzymes that synthesize a variety of polyketide natural products by performing polyketide chain extension and β-keto group modification reactions. We determined the 2.4-angstrom-resolution x-ray crystal structure and the 3.1-angstrom-resolution cryo–electron microscopy structure of the Lsd14 polyketide synthase, stalled at the transacylation and condensation steps, respectively. These structures revealed how the constituent domains are positioned relative to each other, how they rearrange depending on the step in the reaction cycle, and the specific interactions formed between the domains. Like the evolutionarily related mammalian fatty acid synthase, Lsd14 contains two reaction chambers, but only one chamber in Lsd14 has the full complement of catalytic domains, indicating that only one chamber produces the polyketide product at any given time.