Ontology highlight
ABSTRACT:
SUBMITTER: Fischer M
PROVIDER: S-EPMC6972935 | biostudies-literature | 2020 Jan
REPOSITORIES: biostudies-literature
Fischer Manuel M Joppe Mirko M Mulinacci Barbara B Vollrath Ronnald R Konstantinidis Kosta K Kötter Peter P Ciccarelli Luciano L Vonck Janet J Oesterhelt Dieter D Grininger Martin M
Scientific reports 20200121 1
The yeast fatty acid synthase (FAS) is a barrel-shaped 2.6 MDa complex. Upon barrel-formation, two multidomain subunits, each more than 200 kDa large, intertwine to form a heterododecameric complex that buries 170,000 Å<sup>2</sup> of protein surface. In spite of the rich knowledge about yeast FAS in structure and function, its assembly remained elusive until recently, when co-translational interaction of the β-subunit with the nascent α-subunit was found to initiate assembly. Here, we character ...[more]