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Volumn 18, Issue 1, 2009, Pages 240-246

Structural modification of acyl carrier protein by butyryl group

Author keywords

Acyl carrier protein; NMR; Protein structure; Type II fatty acid synthase

Indexed keywords

ACYL CARRIER PROTEIN; PANTETHEINE PHOSPHATE;

EID: 58149471085     PISSN: 09618368     EISSN: 1469896X     Source Type: Journal    
DOI: 10.1002/pro.11     Document Type: Article
Times cited : (31)

References (32)
  • 1
    • 0036079707 scopus 로고    scopus 로고
    • Forty years of bacterial fatty acid synthesis
    • Rock CO, Jackowski S (2002) Forty years of bacterial fatty acid synthesis. Biochem Biophys Res Commun 292:1155-1166.
    • (2002) Biochem Biophys Res Commun , vol.292 , pp. 1155-1166
    • Rock, C.O.1    Jackowski, S.2
  • 2
    • 22244466130 scopus 로고    scopus 로고
    • The structural biology of type II fatty acid biosynthesis
    • White SW, Zheng J, Zhang YM, Rock CO (2005) The structural biology of type II fatty acid biosynthesis. Annu Rev Biochem 74:791-831.
    • (2005) Annu Rev Biochem , vol.74 , pp. 791-831
    • White, S.W.1    Zheng, J.2    Zhang, Y.M.3    Rock, C.O.4
  • 3
    • 0023654454 scopus 로고
    • 3-hydroxymyristoyl)-N-acetylglucosamine
    • 3-hydroxymyristoyl)-N-acetylglucosamine. J Biol Chem 262:5159-5169.
    • (1987) J Biol Chem , vol.262 , pp. 5159-5169
    • Anderson, M.S.1    Raetz, C.R.2
  • 4
    • 0020351537 scopus 로고
    • Regulation of phospholipid synthesis in Escherichia coli. Composition of the acyl-acyl carrier protein pool in vivo
    • Rock CO, Jackowski S (1982) Regulation of phospholipid synthesis in Escherichia coli. Composition of the acyl-acyl carrier protein pool in vivo. J Biol Chem 257:10759-10765.
    • (1982) J Biol Chem , vol.257 , pp. 10759-10765
    • Rock, C.O.1    Jackowski, S.2
  • 5
    • 0026432638 scopus 로고
    • Activation of Escherichia coli prohaemolysin to the mature toxin by acyl carrier protein-dependent fatty acylation
    • Issartel JP, Koronakis V, Hughes C (1991) Activation of Escherichia coli prohaemolysin to the mature toxin by acyl carrier protein-dependent fatty acylation. Nature 351:759-761.
    • (1991) Nature , vol.351 , pp. 759-761
    • Issartel, J.P.1    Koronakis, V.2    Hughes, C.3
  • 6
    • 0033955033 scopus 로고    scopus 로고
    • Holo-(acyl carrier protein) synthase and phosphopantetheinyl transfer in Escherichia coli
    • Flugel RS, Hwangbo Y, Lambalot RH, Cronan JE, Jr, Walsh CT (2000) Holo-(acyl carrier protein) synthase and phosphopantetheinyl transfer in Escherichia coli. J Biol Chem 275:959-968.
    • (2000) J Biol Chem , vol.275 , pp. 959-968
    • Flugel, R.S.1    Hwangbo, Y.2    Lambalot, R.H.3    Cronan Jr, J.E.4    Walsh, C.T.5
  • 7
    • 0034662753 scopus 로고    scopus 로고
    • Crystal structures of substrate binding to Bacillus subtilis holo-(acyl carrier protein) synthase reveal a novel trimeric arrangement of molecules resulting in three active sites
    • Parris KD, Lin L, Tam A, Mathew R, Hixon J, Stahl M, Fritz CC, Seehra J, Somers WS (2000) Crystal structures of substrate binding to Bacillus subtilis holo-(acyl carrier protein) synthase reveal a novel trimeric arrangement of molecules resulting in three active sites. Structure Fold Des 8:883-895.
    • (2000) Structure Fold Des , vol.8 , pp. 883-895
    • Parris, K.D.1    Lin, L.2    Tam, A.3    Mathew, R.4    Hixon, J.5    Stahl, M.6    Fritz, C.C.7    Seehra, J.8    Somers, W.S.9
  • 8
    • 0346101746 scopus 로고    scopus 로고
    • Key residues responsible for acyl carrier protein and beta-ketoacyl-acyl carrier protein reductase (FabG) interaction
    • Zhang YM, Wu B, Zheng J, Rock CO (2003) Key residues responsible for acyl carrier protein and beta-ketoacyl-acyl carrier protein reductase (FabG) interaction. J Biol Chem 278:52935-52943.
    • (2003) J Biol Chem , vol.278 , pp. 52935-52943
    • Zhang, Y.M.1    Wu, B.2    Zheng, J.3    Rock, C.O.4
  • 9
    • 0023813070 scopus 로고
    • Three-dimensional structure of acyl carrier protein determined by NMR pseudoenergy and distance geometry calculations
    • Holak TA, Kearsley SK, Kim Y, Prestegard JH (1988) Three-dimensional structure of acyl carrier protein determined by NMR pseudoenergy and distance geometry calculations. Biochemistry 27:6135-6142.
    • (1988) Biochemistry , vol.27 , pp. 6135-6142
    • Holak, T.A.1    Kearsley, S.K.2    Kim, Y.3    Prestegard, J.H.4
  • 10
    • 0024435205 scopus 로고
    • A dynamic model for the structure of acyl carrier protein in solution
    • Kim Y, Prestegard JH (1989) A dynamic model for the structure of acyl carrier protein in solution. Biochemistry 28:8792-8797.
    • (1989) Biochemistry , vol.28 , pp. 8792-8797
    • Kim, Y.1    Prestegard, J.H.2
  • 11
    • 0037472114 scopus 로고    scopus 로고
    • Solution structure and backbone dynamics of the holo form of the frenolicin acyl carrier protein
    • Li Q, Khosla C, Puglisi JD, Liu CW (2003) Solution structure and backbone dynamics of the holo form of the frenolicin acyl carrier protein. Biochemistry 42:4648-4657.
    • (2003) Biochemistry , vol.42 , pp. 4648-4657
    • Li, Q.1    Khosla, C.2    Puglisi, J.D.3    Liu, C.W.4
  • 12
    • 0037013187 scopus 로고    scopus 로고
    • The solution structure of acyl carrier protein from Mycobacterium tuberculosis
    • Wong HC, Liu G, Zhang YM, Rock CO, Zheng J (2002) The solution structure of acyl carrier protein from Mycobacterium tuberculosis. J Biol Chem 277:15874-15880.
    • (2002) J Biol Chem , vol.277 , pp. 15874-15880
    • Wong, H.C.1    Liu, G.2    Zhang, Y.M.3    Rock, C.O.4    Zheng, J.5
  • 15
    • 0030972114 scopus 로고    scopus 로고
    • Solution structure of the actinorhodin polyketide synthase acyl carrier protein from Streptomyces coelicolor A3(2)
    • Crump MP, Crosby J, Dempsey CE, Parkinson JA, Murray M, Hopwood DA, Simpson TJ (1997) Solution structure of the actinorhodin polyketide synthase acyl carrier protein from Streptomyces coelicolor A3(2). Biochemistry 36:6000-6008.
    • (1997) Biochemistry , vol.36 , pp. 6000-6008
    • Crump, M.P.1    Crosby, J.2    Dempsey, C.E.3    Parkinson, J.A.4    Murray, M.5    Hopwood, D.A.6    Simpson, T.J.7
  • 16
    • 0034656331 scopus 로고    scopus 로고
    • Solution structure of PCP, a prototype for the peptidyl carrier domains of modular peptide synthetases
    • Weber T, Baumgartner R, Renner C, Marahiel MA, Holak TA (2000) Solution structure of PCP, a prototype for the peptidyl carrier domains of modular peptide synthetases. Structure Fold Des 8:407-418.
    • (2000) Structure Fold Des , vol.8 , pp. 407-418
    • Weber, T.1    Baumgartner, R.2    Renner, C.3    Marahiel, M.A.4    Holak, T.A.5
  • 17
    • 0025613125 scopus 로고
    • Refinement of the NMR structures for acyl carrier protein with scalar coupling data
    • Kim Y, Prestegard JH (1990) Refinement of the NMR structures for acyl carrier protein with scalar coupling data. Proteins 8:377-385.
    • (1990) Proteins , vol.8 , pp. 377-385
    • Kim, Y.1    Prestegard, J.H.2
  • 18
    • 0027569483 scopus 로고
    • Amino acid type determination in the sequential assignment procedure of uniformly 13C/15N-enriched proteins
    • Grzesiek S, Bax A (1993) Amino acid type determination in the sequential assignment procedure of uniformly 13C/15N-enriched proteins. J Biomol NMR 3:185-204.
    • (1993) J Biomol NMR , vol.3 , pp. 185-204
    • Grzesiek, S.1    Bax, A.2
  • 19
    • 0028823713 scopus 로고
    • Structures of protein complexes by multidimensional heteronuclear magnetic resonance spectroscopy
    • Gronenborn AM, Clore GM (1995) Structures of protein complexes by multidimensional heteronuclear magnetic resonance spectroscopy. Crit Rev Biochem Mol Biol 30:351-385.
    • (1995) Crit Rev Biochem Mol Biol , vol.30 , pp. 351-385
    • Gronenborn, A.M.1    Clore, G.M.2
  • 21
    • 0026089657 scopus 로고
    • Efficient computation of three-dimensional protein structures in solution from nuclear magnetic resonance data using the program DIANA and the supporting programs CALIBA, HABAS and GLOMSA
    • Guntert P, Braun W, Wuthrich K (1991) Efficient computation of three-dimensional protein structures in solution from nuclear magnetic resonance data using the program DIANA and the supporting programs CALIBA, HABAS and GLOMSA. J Mol Biol 217:517-530.
    • (1991) J Mol Biol , vol.217 , pp. 517-530
    • Guntert, P.1    Braun, W.2    Wuthrich, K.3
  • 22
  • 23
    • 0020475449 scopus 로고
    • A simple method for displaying the hydropathic character of a protein
    • Kyte J, Doolittle RF (1982) A simple method for displaying the hydropathic character of a protein. J Mol Biol 157:105-132.
    • (1982) J Mol Biol , vol.157 , pp. 105-132
    • Kyte, J.1    Doolittle, R.F.2
  • 25
    • 33744954170 scopus 로고    scopus 로고
    • Solution structures of conformationally equilibrium forms of holo-acyl carrier protein (PfACP) from Plasmodium falciparum provides insight into the mechanism of activation of ACPs
    • Sharma AK, Sharma SK, Surolia A, Surolia N, Sarma SP (2006) Solution structures of conformationally equilibrium forms of holo-acyl carrier protein (PfACP) from Plasmodium falciparum provides insight into the mechanism of activation of ACPs. Biochemistry 45:6904-6916.
    • (2006) Biochemistry , vol.45 , pp. 6904-6916
    • Sharma, A.K.1    Sharma, S.K.2    Surolia, A.3    Surolia, N.4    Sarma, S.P.5
  • 26
    • 0035896547 scopus 로고    scopus 로고
    • Identification and analysis of the acyl carrier protein (ACP) docking site on beta-ketoacyl-ACP synthase III
    • Zhang YM, Rao MS, Heath RJ, Price AC, Olson AJ, Rock CO, White SW (2001) Identification and analysis of the acyl carrier protein (ACP) docking site on beta-ketoacyl-ACP synthase III. J Biol Chem 276:8231-8238.
    • (2001) J Biol Chem , vol.276 , pp. 8231-8238
    • Zhang, Y.M.1    Rao, M.S.2    Heath, R.J.3    Price, A.C.4    Olson, A.J.5    Rock, C.O.6    White, S.W.7
  • 27
    • 0037238269 scopus 로고    scopus 로고
    • The application of computational methods to explore the diversity and structure of bacterial fatty acid synthase
    • Zhang YM, Marrakchi H, White SW, Rock CO (2003) The application of computational methods to explore the diversity and structure of bacterial fatty acid synthase. J Lipid Res 44:1-10.
    • (2003) J Lipid Res , vol.44 , pp. 1-10
    • Zhang, Y.M.1    Marrakchi, H.2    White, S.W.3    Rock, C.O.4
  • 31
    • 58149463562 scopus 로고    scopus 로고
    • Goddard TD, Kneller DG (1998) SPARKY, 3.0. San Francisco: University of California.
    • Goddard TD, Kneller DG (1998) SPARKY, 3.0. San Francisco: University of California.
  • 32
    • 0031576336 scopus 로고    scopus 로고
    • Torsion angle dynamics for NMR structure calculation with the new program DYANA
    • Guntert P, Mumenthaler C, Wuthrich K (1997) Torsion angle dynamics for NMR structure calculation with the new program DYANA. J Mol Biol 273:283-298.
    • (1997) J Mol Biol , vol.273 , pp. 283-298
    • Guntert, P.1    Mumenthaler, C.2    Wuthrich, K.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.