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The Crystal Structure of a Mammalian Fatty Acid Synthase
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.
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Fatty acid synthase and the lipogenic phenotype in cancer pathogenesis
Menendez, J. A., & Lupu, R. (2007) · Nature Reviews Cancer · doi:10.1038/nrc2222 · Cited by 2,941
Principles of protein-protein interactions
Jones, S., & Thornton, J. M. (1996) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.93.1.13 · Cited by 2,684
Fatty acid synthesis: a potential selective target for antineoplastic therapy
Kuhajda, F. P., Jenner, K., Wood, F. D., Hennigar, R. A., Jacobs, L. B., Dick, J. D., & Pasternack, G. R. (1994) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.91.14.6379 · Cited by 705
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The multifaceted roles of fatty acid synthesis in cancer
Röhrig, F., & Schulze, A. (2016) · Nature Reviews Cancer · doi:10.1038/nrc.2016.89 · Cited by 1,651
De novo fatty-acid synthesis and related pathways as molecular targets for cancer therapy
Mashima, T., Seimiya, H., & Tsuruo, T. (2009) · British Journal of Cancer · doi:10.1038/sj.bjc.6605007 · Cited by 555
Nonribosomal peptide synthetases: structures and dynamics
Strieker, M., Tanović, A., & Marahiel, M. A. (2010) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2010.01.009 · Cited by 441
Fatty acid synthase and liver triglyceride metabolism: Housekeeper or messenger?
Jensen-Urstad, A. P. L., & Semenkovich, C. F. (2012) · Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids · doi:10.1016/j.bbalip.2011.09.017 · Cited by 406
Lipid Catabolism via CPT1 as a Therapeutic Target for Prostate Cancer
Schlaepfer, I. R., Rider, L., Rodrigues, L. U., Gijón, M. A., Pac, C. T., Romero, L., Cimic, A., Sirintrapun, S. J., Glodé, L. M., Eckel, R. H., et al. (2014) · Molecular Cancer Therapeutics · doi:10.1158/1535-7163.mct-14-0183 · Cited by 304
Metadata
- Authors
- Maier, T., Leibundgut, M., & Ban, N.
- Venue
- Science
- Published
- 2008-09-05
- Volume
- 321
- Issue
- 5894
- Pages
- 1315-1322
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- OpenAlex
- W2054474037
- Cited by
- 505
- References
- 3
- FWCI
- 10.31
- Type
- journal article
- Language
- en
- Open access
- closed
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