Rxivist logo

Rxivist combines preprints from bioRxiv with data from Twitter to help you find the papers being discussed in your field. Currently indexing 60,207 bioRxiv papers from 267,649 authors.

Gating Mechanism of β-Ketoacyl-ACP Synthases

By Jeffrey T. Mindrebo, Ashay Patel, Woojoo E. Kim, Tony D. Davis, Aochiu Chen, Thomas G. Bartholow, James J. La Clair, J. Andrew McCammon, Joseph P. Noel, Michael Burkart

Posted 21 May 2019
bioRxiv DOI: 10.1101/644518

Formation of carbon-carbon bonds via β-ketoacyl-acyl carrier protein (ACP) synthases (KS), are key reactions during de novo fatty acid and polyketide biosynthesis. KSs recognize multiple ACPs and choreograph ping-pong mechanisms often in an iterative fashion. Therefore, KSs must limit non-productive protein-protein interactions (PPIs) to achieve high degrees of reaction fidelity. To better understand the stereochemical features governing substrate discrimination during ACP-KS PPIs, we determined x-ray crystal structures complemented by molecular dynamic simulations of E. coli AcpP in complex with the elongating KSs, FabF and FabB. Covalently trapped substrate analogs were used to interrogate critical catalytic events accompanying carbon-carbon bond formation revealing a previously unknown gating mechanism during the binding and delivery of acyl-AcpPs. Two active site loops undergo large conformational excursions during this dynamic gating mechanism and are likely evolutionarily conserved features generally in elongating KSs.

Download data

  • Downloaded 292 times
  • Download rankings, all-time:
    • Site-wide: 32,226 out of 60,207
    • In biochemistry: 839 out of 1,745
  • Year to date:
    • Site-wide: 10,334 out of 60,207
  • Since beginning of last month:
    • Site-wide: 16,854 out of 60,207

Altmetric data

Downloads over time

Distribution of downloads per paper, site-wide

Sign up for the Rxivist weekly newsletter! (Click here for more details.)