Structure of fungal fatty acid synthase and implications for iterative substrate shuttling

Science

Volumn 316, Issue 5822, 2007, Pages 254-261

  Jenni, Simon ^a   Leibundgut, Marc ^a   Boehringer, Daniel ^a   Frick, Christian ^a   Mikolásek, Bohdan ^a   Ban, Nenad ^a  

^a ETH ZURICH   (Switzerland)

Author keywords

[No Author keywords available]

Indexed keywords

FATTY ACID SYNTHASE; FUNGAL ENZYME;

ENZYME ACTIVITY; FATTY ACID; FUNGUS; PROTEIN;

ALPHA CHAIN; ARTICLE; BETA CHAIN; CRYSTAL STRUCTURE; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME ANALYSIS; ENZYME SPECIFICITY; ENZYME STRUCTURE; ENZYME SUBSTRATE; FATTY ACID SYNTHESIS; FUNGUS; NONHUMAN; PRIORITY JOURNAL; THERMOMYCES LANUGINOSUS;

3-OXOACYL-(ACYL-CARRIER-PROTEIN) SYNTHASE; ACETYLTRANSFERASES; ACYL CARRIER PROTEIN; ACYLTRANSFERASES; AMINO ACID SEQUENCE; ASCOMYCOTA; CATALYTIC DOMAIN; CRYSTALLOGRAPHY, X-RAY; ENOYL-(ACYL-CARRIER-PROTEIN) REDUCTASE (NADH); FATTY ACID SYNTHETASE COMPLEX; FUNGAL PROTEINS; HYDRO-LYASES; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; NADP; PROTEIN CONFORMATION; PROTEIN SUBUNITS; SUBSTRATE SPECIFICITY;

THERMOMYCES LANUGINOSUS;

EID: 34247383568     PISSN: 00368075     EISSN: 10959203     Source Type: Journal    
DOI: 10.1126/science.1138248     Document Type: Article

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42. All data were collected at the Swiss Light Source (SLS, Paul Scherrer Institute, Villigen). We are grateful to C. Schulze-Briese, S. Gutmann, E. Pohl, S. Russo, and T. Tomizaki for their outstanding support at the 5L5. We thank T. Maier and J. Erzberger for critically reading the manuscript and all members of the Ban laboratory for suggestions and discussions; R. Grosse-Kunstleve, P. Afonine, and P. Adams for providing a prerelease version of the PHENIX refinement program and advice regarding structure refinement; A. Jones for a prerelease version of the program O; and D. Sargent for technical assistance. We thank A. Tsang for assembling T. lanuginsosus FAS contigs from expressed sequence tag sequence data produced by the Fungal Genomics Project (https://fungalgenomics.concordia.ca). This work was supported by the Swiss National Science Foundation (SNSF) and the National Center of Excellence in Research (NCCR) Structural Biology program of the SNSF. D.B. was supported by a Federation of European Biochemical Societies long-term fellowship. We thank the Electron Microscopy Center Zurich (EMEZ) for support. Coordinates and structure factors of the T. lanuginosus crystal structures have been deposited in the Protein Data Bank with accession codes 2UV9, 2UVA, 2UVB, and 2UVC. The cryoelectron microscopy map has been deposited at the EM Data Bank with accession code EMD-1338.