6WC7

Acyl carrier protein (ACP) domain bound to dehydratase (DH) domain in fungal fatty acid synthase (FAS)

Summary for 6WC7

• Entry DOI: 10.2210/pdb6wc7/pdb
• EMDB information: 21602
• Descriptor: Fatty acid synthase subunit beta, Fatty acid synthase subunit alpha (2 entities in total)
• Functional Keywords: fatty acid synthase, acyl carrier protein, dehydratase, biosynthetic protein, transferase
• Biological source: Saccharomyces cerevisiae (Baker's yeast); More
• Total number of polymer chains: 2
• Total formula weight: 436953.64

Authors

Lou, J.W.,Mazhab-Jafari, M.T. (deposition date: 2020-03-29, release date: 2020-06-03, Last modification date: 2024-03-06)

Primary citation

Lou, J.W.,Mazhab-Jafari, M.T.
Steric occlusion regulates proximal interactions of acyl carrier protein domain in fungal fatty acid synthase.
Commun Biol, 3:274-274, 2020

PubMed Abstract: The acyl carrier protein (ACP) domain shuttles substrates and reaction intermediates in type I fungal fatty acid synthases via transient protein-protein interactions. Here, using electron cryo-microscopy (cryoEM), we report the structure of a fungal FAS stalled at the dehydration reaction, which precedes the final enoyl reduction in the fatty acid biosynthesis cycle. This conformation revealed multiple contact sites between ACP and the dehydratase (DH) and enoyl reductase (ER) domains that occluded the ACP binding to the adjacent ER domain. Our data suggests a minimal path from the DH to the ER reaction site that requires minute changes in the coordinates of the structured N- and C- termini of the ACP domain.

PubMed: 32471977
DOI: 10.1038/s42003-020-0997-y

Experimental method

ELECTRON MICROSCOPY (5.8 Å)