The Crystal Structure of a Mammalian Fatty Acid Synthase Export

@article{citeulike:4845136, abstract = {Mammalian fatty acid synthase is a large multienzyme that catalyzes all steps of fatty acid synthesis. We have determined its crystal structure at 3.2 angstrom resolution covering five catalytic domains, whereas the flexibly tethered terminal acyl carrier protein and thioesterase domains remain unresolved. The structure reveals a complex architecture of alternating linkers and enzymatic domains. Substrate shuttling is facilitated by flexible tethering of the acyl carrier protein domain and by the limited contact between the condensing and modifying portions of the multienzyme, which are mainly connected by linkers rather than direct interaction. The structure identifies two additional nonenzymatic domains: (i) a pseudo-ketoreductase and (ii) a peripheral pseudo-methyltransferase that is probably a remnant of an ancestral methyltransferase domain maintained in some related polyketide synthases. The structural comparison of mammalian fatty acid synthase with modular polyketide synthases shows how their segmental construction allows the variation of domain composition to achieve diverse product synthesis. 10.1126/science.1161269}, author = {Maier, Timm and Leibundgut, Marc and Ban, Nenad}, citeulike-article-id = {4845136}, citeulike-linkout-0 = {http://dx.doi.org/10.1126/science.1161269}, citeulike-linkout-1 = {http://www.sciencemag.org/cgi/content/abstract/321/5894/1315}, citeulike-linkout-2 = {http://view.ncbi.nlm.nih.gov/pubmed/18772430}, citeulike-linkout-3 = {http://www.hubmed.org/display.cgi?uids=18772430}, doi = {10.1126/science.1161269}, journal = {Science}, keywords = {fasi, mammalian, strucutre}, month = {September}, number = {5894}, pages = {1315--1322}, posted-at = {2009-06-14 13:26:35}, priority = {2}, title = {The Crystal Structure of a Mammalian Fatty Acid Synthase}, url = {http://dx.doi.org/10.1126/science.1161269}, volume = {321}, year = {2008} }

TY - JOUR ID - citeulike:4845136 L3 - citeulike-article-id:4845136 N2 - Mammalian fatty acid synthase is a large multienzyme that catalyzes all steps of fatty acid synthesis. We have determined its crystal structure at 3.2 angstrom resolution covering five catalytic domains, whereas the flexibly tethered terminal acyl carrier protein and thioesterase domains remain unresolved. The structure reveals a complex architecture of alternating linkers and enzymatic domains. Substrate shuttling is facilitated by flexible tethering of the acyl carrier protein domain and by the limited contact between the condensing and modifying portions of the multienzyme, which are mainly connected by linkers rather than direct interaction. The structure identifies two additional nonenzymatic domains: (i) a pseudo-ketoreductase and (ii) a peripheral pseudo-methyltransferase that is probably a remnant of an ancestral methyltransferase domain maintained in some related polyketide synthases. The structural comparison of mammalian fatty acid synthase with modular polyketide synthases shows how their segmental construction allows the variation of domain composition to achieve diverse product synthesis. 10.1126/science.1161269 IS - 5894 JF - Science EP - 1322 TI - The Crystal Structure of a Mammalian Fatty Acid Synthase VL - 321 SP - 1315 KW - fasi KW - mammalian KW - strucutre AU - Maier, Timm AU - Leibundgut, Marc AU - Ban, Nenad PY - 2008/09/05/ UR - http://dx.doi.org/10.1126/science.1161269 ER -