Architecture of mammalian fatty acid synthase at 4.5 å resolution

Science

Volumn 311, Issue 5765, 2006, Pages 1258-1262

  Maier, Timm ^a   Jenni, Simon ^a   Ban, Nenad ^a  

^a ETH ZURICH   (Switzerland)

Author keywords

[No Author keywords available]

Indexed keywords

CARRIER CONCENTRATION; CARRIER MOBILITY; CATALYSIS; CELLS; CONFORMATIONS; CRYSTAL STRUCTURE; ENZYMES; NATURAL SCIENCES; POLYPEPTIDES;

ACTIVE SITES; ACYL CARRIER; CATALYTIC DOMAINS; CHAIN CARRIES; CHAMBERS; COMPLEX ARCHITECTURE; CYCLIC ELONGATION; HOMOLOGOUS TEMPLATE; MAMMALIAN; MULTIENZYMES;

FATTY ACIDS;

ACYL CARRIER PROTEIN; FATTY ACID; FATTY ACID SYNTHASE; POLYPEPTIDE;

ENZYME ACTIVITY; FATTY ACID; MAMMAL;

ARTICLE; COMPLEX FORMATION; ELECTRON; ENZYME ACTIVE SITE; ENZYME CONFORMATION; ENZYME STRUCTURE; FATTY ACID SYNTHESIS; MAMMAL; NONHUMAN; PRIORITY JOURNAL; PROTEIN DOMAIN; REACTION ANALYSIS; SEQUENCE HOMOLOGY; STRUCTURE ANALYSIS;

ACYL CARRIER PROTEIN; ANIMALS; BINDING SITES; CATALYTIC DOMAIN; CRYSTALLIZATION; CRYSTALLOGRAPHY, X-RAY; DIMERIZATION; FATTY ACID SYNTHETASE COMPLEX; FATTY ACIDS; MAMMARY GLANDS, ANIMAL; MODELS, MOLECULAR; PROTEIN CONFORMATION; PROTEIN FOLDING; PROTEIN STRUCTURE, QUATERNARY; PROTEIN STRUCTURE, SECONDARY; PROTEIN STRUCTURE, TERTIARY; PROTEIN SUBUNITS; SWINE;

MAMMALIA; SUIDAE;

EID: 33644697200     PISSN: 00368075     EISSN: 10959203     Source Type: Journal    
DOI: 10.1126/science.1123248     Document Type: Article

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44. We acknowledge N. Dörwald for technical assistance and B. Blattmann at the National Center of Competence in Research (NCCR) robotic nanoliter crystallization facility for support. Animal material was provided by G. Bearth of the veterinary service, Zürich. Data collection was performed at the Swiss Light Source (SLS) of the Paul Scherrer Institut in Villigen, Switzerland, and at beamline BM14, European Synchrotron Radiation Facility, Grenoble, France. We are grateful to C. Schulze-Briese, A. Wagner, and S. Gutmann (SL5), whose efforts have made these experiments possible. This work was supported by the Swiss National Science Foundation (SNSF) and the NCCR Structural Biology program of the SNSF. Coordinates of the placed homologous domains have been deposited in the Protein Data Bank with accession code 2cf2.