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Literature summary for 2.3.1.85 extracted from

  • Pappenberger, G.; Benz, J.; Gsell, B.; Hennig, M.; Ruf, A.; Stihle, M.; Thoma, R.; Rudolph, M.G.
    Structure of the human fatty acid synthase KS-MAT didomain as a framework for inhibitor design (2010), J. Mol. Biol., 397, 508-519.
    View publication on PubMed

Crystallization (Commentary)

Crystallization (Comment) Organism
high-resolution crystal structure of a large part of human fatty acid synthase that encompasses the tandem domain of beta-oxoacyl synthase KS connected by a linker domain to the malonyltransferase domain MAT, to 2.15 A resolution. Hinge regions that allow for substantial flexibility of the subdomains are defined. The KS domain forms the canonical dimer, and its substrate-binding site geometry differs markedly from that of bacterial homologues but is similar to that of the porcine orthologue. The didomain structure reveals a possible way to generate a small and compact KS domain by omitting a large part of the linker and MAT domains, which could greatly aid in rapid screening of KS inhibitors. In the crystal, the MAT domain exhibits two closed conformations that differ significantly by rigid-body plasticity Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens P49327
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