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Literature summary for 2.3.1.86 extracted from

  • Fischer, M.; Joppe, M.; Mulinacci, B.; Vollrath, R.; Konstantinidis, K.; Koetter, P.; Ciccarelli, L.; Vonck, J.; Oesterhelt, D.; Grininger, M.
    Analysis of the co-translational assembly of the fungal fatty acid synthase (FAS) (2020), Sci. Rep., 10, 895 .
    View publication on PubMedView publication on EuropePMC
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Organism

Organism UniProt Comment Textmining
Saccharomyces cerevisiae P07149 and P19097 P07149 i.e.subunit FAS1, P19097 i.e. subunit FAS2
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Saccharomyces cerevisiae ATCC 204508 P07149 and P19097 P07149 i.e.subunit FAS1, P19097 i.e. subunit FAS2
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General Information

General Information Comment Organism
metabolism cotranslational assembly of yeast FAS. The N-terminus of subunit alpha (FAS2) intertwines with the C-terminus of subunt beta (FAS1) by getting sandwiched between a structured malonyl-palmitoyl-transferase core fold and a alpha67/alpha68 element. The cotranslationally formed interaction is sensitive to perturbations. The assembly of yeast FAS can also proceed when subunit borders are shifted. Linking subunits of FAS at the cotranslationally formed interface and introducing splitting sites at two other sites, within the alpha-helical bundle structure 4-helical bundle of subunit alpha and within the antiparallel 6-stranded beta-sheet of beta, leads to intact protein. The cotranslational assembly may not be strictly sequence- or site-specific Saccharomyces cerevisiae