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Volumn 107, Issue 20, 2010, Pages 9164-9169

Direct structural insight into the substrate-shuttling mechanism of yeast fatty acid synthase by electron cryomicroscopy

Author keywords

Acyl carrier protein; Cryoelectron microscopy; Fatty acid synthesis; Molecular architecture

Indexed keywords

ACYL CARRIER PROTEIN; FATTY ACID SYNTHASE;

EID: 77952719956     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.0913547107     Document Type: Article
Times cited : (53)

References (29)
  • 1
    • 22244466130 scopus 로고    scopus 로고
    • The structural biology of type II fatty acid biosynthesis
    • DOI 10.1146/annurev.biochem.74.082803.133524
    • White SW, Zheng J, Zhang Y-M, Rock CO (2005) The structural biology of type II fatty acid biosynthesis. Annu Rev Biochem 74:791-831. (Pubitemid 40995524)
    • (2005) Annual Review of Biochemistry , vol.74 , pp. 791-831
    • White, S.W.1    Zheng, J.2    Zhang, Y.-M.3    Rock, C.O.4
  • 3
    • 0037411269 scopus 로고    scopus 로고
    • Structural and functional organization of the animal fatty acid synthase
    • DOI 10.1016/S0163-7827(02)00067-X
    • Smith S, Witkowski A, Joshi AK (2003) Structural and functional organization of the animal fatty acid synthase. Prog Lipid Res 42(4):298-317. (Pubitemid 36411688)
    • (2003) Progress in Lipid Research , vol.42 , Issue.4 , pp. 289-317
    • Smith, S.1    Witkowski, A.2    Joshi, A.K.3
  • 5
    • 17844385334 scopus 로고    scopus 로고
    • Structure and molecular organization of mammalian fatty acid synthase
    • Asturias FJ, et al. (2005) Structure and molecular organization of mammalian fatty acid synthase. Nat Struct Mol Biol 12(3):225-232.
    • (2005) Nat Struct Mol Biol , vol.12 , Issue.3 , pp. 225-232
    • Asturias, F.J.1
  • 6
    • 33644697200 scopus 로고    scopus 로고
    • Architecture of mammalian fatty acid synthase at 4.5 å resolution
    • DOI 10.1126/science.1123248
    • Maier T, Jenni S, Ban N (2006) Architecture of mammalian fatty acid synthase at 4.5 Å resolution. Science 311:1258-1262. (Pubitemid 43334709)
    • (2006) Science , vol.311 , Issue.5765 , pp. 1258-1262
    • Maier, T.1    Jenni, S.2    Ban, N.3
  • 7
    • 59649102440 scopus 로고    scopus 로고
    • Conformational flexibility of metazoan fatty acid synthase enables catalysis
    • Brignole EJ, Smith S, Asturias FJ (2009) Conformational flexibility of metazoan fatty acid synthase enables catalysis. Nat Struct Mol Biol 16(2):190-197.
    • (2009) Nat Struct Mol Biol , vol.16 , Issue.2 , pp. 190-197
    • Brignole, E.J.1    Smith, S.2    Asturias, F.J.3
  • 8
    • 84944295787 scopus 로고
    • Three-dimensional electron microscopy of individual biological objects Part III. Experimental results on yeast fatty acid synthetase
    • Hoppe W, Schramm HJ, Sturm M, Hunsmann N, Gaßmann J (1976) Three-dimensional electron microscopy of individual biological objects Part III. Experimental results on yeast fatty acid synthetase. Z Naturforsch 31a:1380-1390.
    • (1976) Z Naturforsch , vol.31 A , pp. 1380-1390
    • Hoppe, W.1    Schramm, H.J.2    Sturm, M.3    Hunsmann, N.4    Gaßmann, J.5
  • 9
    • 0026628860 scopus 로고
    • Structure-function relationships of the yeast fatty acid synthase: Negative-stain, cryo-electron microscopy, and image analysis studies of the end views of the structure
    • Stoops JK, Kolodziej SJ, Schroeter JP, Bretaudierre J-P, Wakil SJ (1992) Structure-function relationships of the yeast fatty acid synthase: Negative-stain, cryo-electron microscopy, and image analysis studies of the end views of the structure. Proc Natl Acad Sci USA 89:6585-6589.
    • (1992) Proc Natl Acad Sci USA , vol.89 , pp. 6585-6589
    • Stoops, J.K.1    Kolodziej, S.J.2    Schroeter, J.P.3    Bretaudierre, J.-P.4    Wakil, S.J.5
  • 10
    • 0029904850 scopus 로고    scopus 로고
    • Structure-function relationships of the Saccharomyces cerevisiae fatty acid synthase
    • Kolodziej SJ, Penczek PA, Schroeter JP, Stoops JK (1996) Structure-function relationships of the Saccharomyces cerevisiae fatty acid synthase. J Biol Chem 271 (45):28422-28429.
    • (1996) J Biol Chem , vol.271 , Issue.45 , pp. 28422-28429
    • Kolodziej, S.J.1    Penczek, P.A.2    Schroeter, J.P.3    Stoops, J.K.4
  • 11
    • 34247383568 scopus 로고    scopus 로고
    • Structure of fungal fatty acid synthase and implications for iterative substrate shuttling
    • DOI 10.1126/science.1138248
    • Jenni S, et al. (2007) Structure of fungal fatty acid synthase and implications for iterative substrate shuttling. Science 316:254-261. (Pubitemid 46633098)
    • (2007) Science , vol.316 , Issue.5822 , pp. 254-261
    • Jenni, S.1    Leibundgut, M.2    Boehringer, D.3    Frick, C.4    Mikolasek, B.5    Ban, N.6
  • 12
    • 34247353309 scopus 로고    scopus 로고
    • Structural basis for substrate delivery by acyl carrier protein in the yeast fatty acid synthase
    • DOI 10.1126/science.1138249
    • Leibundgut M, Jenni S, Frick C, Ban N (2007) Structural basis for substrate delivery by acyl carrier protein in the yeast fatty acid synthase. Science 316:288-290. (Pubitemid 46633107)
    • (2007) Science , vol.316 , Issue.5822 , pp. 288-290
    • Leibundgut, M.1    Jenni, S.2    Frick, C.3    Ban, N.4
  • 13
    • 34147098650 scopus 로고    scopus 로고
    • The Crystal Structure of Yeast Fatty Acid Synthase, a Cellular Machine with Eight Active Sites Working Together
    • DOI 10.1016/j.cell.2007.03.013, PII S0092867407003297
    • Lomakin IB, Xiong Y, Steitz TA (2007) The crystal structure of yeast fatty acid synthase, a cellular machine with eight active sites working together. Cell 129:319-332. (Pubitemid 46574968)
    • (2007) Cell , vol.129 , Issue.2 , pp. 319-332
    • Lomakin, I.B.1    Xiong, Y.2    Steitz, T.A.3
  • 14
    • 51349099946 scopus 로고    scopus 로고
    • Inhibition of the fungal fatty acid synthase type I multienzyme complex
    • Johansson P, et al. (2008) Inhibition of the fungal fatty acid synthase type I multienzyme complex. Proc Natl Acad Sci USA 105(35):12803-12808.
    • (2008) Proc Natl Acad Sci USA , vol.105 , Issue.35 , pp. 12803-12808
    • Johansson, P.1
  • 15
    • 0022412624 scopus 로고
    • Yeast fatty acid synthase: Structure to function relationship
    • DOI 10.1021/bi00344a044
    • Singh N, Wakil SJ, Stoops JK (1985) Yeast fatty acid synthase: Structure to function relationship. Biochemistry 24:6598-6602. (Pubitemid 16207137)
    • (1985) Biochemistry , vol.24 , Issue.23 , pp. 6598-6602
    • Singh, N.1    Wakil, S.J.2    Stoops, J.K.3
  • 16
    • 9244234513 scopus 로고    scopus 로고
    • Biosynthesis of nonribosomal peptides
    • Finking R, Marahiel MA (2004) Biosynthesis of nonribosomal peptides. Annu Rev Microbiol 58:453-488.
    • (2004) Annu Rev Microbiol , vol.58 , pp. 453-488
    • Finking, R.1    Marahiel, M.A.2
  • 17
    • 38849098884 scopus 로고    scopus 로고
    • Acyl carrier protein: Structure-function relationships in a conserved multifunctional protein family
    • Byers DM, Gong H (2007) Acyl carrier protein: Structure-function relationships in a conserved multifunctional protein family. Biochem Cell Biol 85:649-662.
    • (2007) Biochem Cell Biol , vol.85 , pp. 649-662
    • Byers, D.M.1    Gong, H.2
  • 18
    • 0033377664 scopus 로고    scopus 로고
    • EMAN: Semiautomated software for high-resolution single-particle reconstructions
    • Ludtke SJ, Baldwin PR, Chiu W (1999) EMAN: Semiautomated software for high-resolution single-particle reconstructions. J Struct Biol 128:82-97.
    • (1999) J Struct Biol , vol.128 , pp. 82-97
    • Ludtke, S.J.1    Baldwin, P.R.2    Chiu, W.3
  • 19
    • 1842409555 scopus 로고    scopus 로고
    • Determination of the fold of the core protein of hepatitis B virus by electron cryomicroscopy
    • DOI 10.1038/386088a0
    • Böttcher B, Wynne SA, Crowther RA (1997) Determination of the fold of the core protein of hepatitis B virus by electron cryomicroscopy. Nature 386:88-91. (Pubitemid 27130926)
    • (1997) Nature , vol.386 , Issue.6620 , pp. 88-91
    • Bottcher, B.1    Wynne, S.A.2    Crowther, R.A.3
  • 20
    • 0142042865 scopus 로고    scopus 로고
    • Optimal determination of particle orientation, absolute hand, and contrast loss in single-particle electron cryomicroscopy
    • DOI 10.1016/j.jmb.2003.07.013
    • Rosenthal P, Henderson R (2003) Optimal determination of particle orientation, absolute hand, and contrast loss in single-particle electron cryomicroscopy. J Mol Biol 333:721-745. (Pubitemid 37268015)
    • (2003) Journal of Molecular Biology , vol.333 , Issue.4 , pp. 721-745
    • Rosenthal, P.B.1    Henderson, R.2
  • 21
    • 4444221565 scopus 로고    scopus 로고
    • UCSF Chimera: A visualisation system for exploratory research and analysis
    • Pettersen EF, et al. (2004) UCSF Chimera: A visualisation system for exploratory research and analysis. J Comput Chem 25:1605-1612.
    • (2004) J Comput Chem , vol.25 , pp. 1605-1612
    • Pettersen, E.F.1
  • 22
    • 68149138671 scopus 로고    scopus 로고
    • Multimeric options for the auto-activation of the fungal FAS type I megasynthase
    • Johansson P, et al. (2009) Multimeric options for the auto-activation of the fungal FAS type I megasynthase. Structure 17(8):1063-1074.
    • (2009) Structure , vol.17 , Issue.8 , pp. 1063-1074
    • Johansson, P.1
  • 23
    • 33644847296 scopus 로고    scopus 로고
    • Estimation of variance in single-particle reconstruction using the bootstrap technique
    • Penczek PA, Yang C, Frank J, Spahn CMT (2006) Estimation of variance in single-particle reconstruction using the bootstrap technique. J Struct Biol 154(1):168-183.
    • (2006) J Struct Biol , vol.154 , Issue.1 , pp. 168-183
    • Penczek, P.A.1    Yang, C.2    Frank, J.3    Spahn, C.M.T.4
  • 24
    • 33646042904 scopus 로고    scopus 로고
    • A method of focused classification, based on the bootstrap 3D variance analysis, and its application to EF-G-dependent translocation
    • Penczek PA, Frank J, Spahn CMT (2006) A method of focused classification, based on the bootstrap 3D variance analysis, and its application to EF-G-dependent translocation. J Struct Biol 154(1):184-194.
    • (2006) J Struct Biol , vol.154 , Issue.1 , pp. 184-194
    • Penczek, P.A.1    Frank, J.2    Spahn, C.M.T.3
  • 25
    • 59649106114 scopus 로고    scopus 로고
    • Cryo-EM structure of the native GroEL-GroES complex from Thermus thermophilus encapsulating substrate inside the cavity
    • Kanno R, Koike-Takeshita A, Yokoyama K, Taguchi H, Mitsuoka K (2009) Cryo-EM structure of the native GroEL-GroES complex from Thermus thermophilus encapsulating substrate inside the cavity. Structure 17:287-293.
    • (2009) Structure , vol.17 , pp. 287-293
    • Kanno, R.1    Koike-Takeshita, A.2    Yokoyama, K.3    Taguchi, H.4    Mitsuoka, K.5
  • 26
    • 63849246525 scopus 로고    scopus 로고
    • Protein structure prediction on the Web: A case study using the Phyre server
    • Kelley LA, Sternberg MJ (2009) Protein structure prediction on the Web: A case study using the Phyre server. Nat Protoc 4:363-371.
    • (2009) Nat Protoc , vol.4 , pp. 363-371
    • Kelley, L.A.1    Sternberg, M.J.2
  • 28
    • 3242886771 scopus 로고    scopus 로고
    • PDB2PQR: An automated pipeline for the setup of Poisson-Boltzmann electrostatics calculations
    • Dolinsky TJ, Nielsen JE, McCammon JA, Baker NA (2004) PDB2PQR: An automated pipeline for the setup of Poisson-Boltzmann electrostatics calculations. Nucleic Acids Res 32:W665-W667.
    • (2004) Nucleic Acids Res , vol.32
    • Dolinsky, T.J.1    Nielsen, J.E.2    McCammon, J.A.3    Baker, N.A.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.