Literature summary for 2.3.1.85 extracted from

Gipson, P.; Mills, D.J.; Wouts, R.; Grininger, M.; Vonck, J.; Kuehlbrandt, W.
Direct structural insight into the substrate-shuttling mechanism of yeast fatty acid synthase by electron cryomicroscopy (2010), Proc. Natl. Acad. Sci. USA, 107, 9164-9169.

Crystallization (Commentary)

Crystallization (Comment)	Organism
three-dimensional map of yeast fatty acid synthase at 5.9 A resolution, obtained by electron cryomicroscopy of single particles. Distinct density regions in the reaction chambers next to each of the catalytic domains fitted the substrate-binding acyl carrier protein domain. In each case, this results in the expected distance of about 18 A from the acyl carrier protein substrate-binding site to the active site of the catalytic domains. The multiple, partially occupied positions of the acyl carrier protein within the reaction chamber provide direct structural insight into the substrate-shuttling mechanism. The acyl carrier protein domain is mobile within the fatty acid synthase barrel, enabling it to visit successive catalytic sites	Saccharomyces cerevisiae

Crystallization (Comment)

Organism

three-dimensional map of yeast fatty acid synthase at 5.9 A resolution, obtained by electron cryomicroscopy of single particles. Distinct density regions in the reaction chambers next to each of the catalytic domains fitted the substrate-binding acyl carrier protein domain. In each case, this results in the expected distance of about 18 A from the acyl carrier protein substrate-binding site to the active site of the catalytic domains. The multiple, partially occupied positions of the acyl carrier protein within the reaction chamber provide direct structural insight into the substrate-shuttling mechanism. The acyl carrier protein domain is mobile within the fatty acid synthase barrel, enabling it to visit successive catalytic sites

Saccharomyces cerevisiae

Organism

Organism	UniProt	Comment	Textmining
Saccharomyces cerevisiae	-	-	-

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Release 2023.1 (January 2023)