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-Structure paper
タイトル | Direct structural insight into the substrate-shuttling mechanism of yeast fatty acid synthase by electron cryomicroscopy. |
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ジャーナル・号・ページ | Proc Natl Acad Sci U S A, Vol. 107, Issue 20, Page 9164-9169, Year 2010 |
掲載日 | 2010年5月18日 |
![]() | Preeti Gipson / Deryck J Mills / Remco Wouts / Martin Grininger / Janet Vonck / Werner Kühlbrandt / ![]() |
PubMed 要旨 | Yeast fatty acid synthase (FAS) is a 2.6-MDa barrel-shaped multienzyme complex, which carries out cyclic synthesis of fatty acids. By electron cryomicroscopy of single particles we obtained a three- ...Yeast fatty acid synthase (FAS) is a 2.6-MDa barrel-shaped multienzyme complex, which carries out cyclic synthesis of fatty acids. By electron cryomicroscopy of single particles we obtained a three-dimensional map of yeast FAS at 5.9-A resolution. Compared to the crystal structures of fungal FAS, the EM map reveals major differences and new features that indicate a considerably different arrangement of the complex in solution compared to the crystal structures, as well as a high degree of variance inside the barrel. Distinct density regions in the reaction chambers next to each of the catalytic domains fitted the substrate-binding acyl carrier protein (ACP) domain. In each case, this resulted in the expected distance of approximately 18 A from the ACP substrate-binding site to the active site of the catalytic domains. The multiple, partially occupied positions of the ACP within the reaction chamber provide direct structural insight into the substrate-shuttling mechanism of fatty acid synthesis in this large cellular machine. |
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手法 | EM (単粒子) |
解像度 | 5.9 Å |
構造データ | ![]() EMDB-1623: |
由来 |
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