메뉴 건너뛰기




Volumn 425, Issue 2, 2013, Pages 365-377

Structural insights into the mechanism and inhibition of the β-hydroxydecanoyl-acyl carrier protein dehydratase from Pseudomonas aeruginosa

Author keywords

bacterial virulence; fatty acid biosynthesis; hydroxydecanoyl ACP dehydratase

Indexed keywords

3 HYDROXYDECANOYL N ACETYLCYSTEAMINE; BACTERIAL PROTEIN; BETA HYDROXYACYL ACYL CARRIER PROTEIN; FABA PROTEIN; FABZ PROTEIN; UNCLASSIFIED DRUG;

EID: 84872111212     PISSN: 00222836     EISSN: 10898638     Source Type: Journal    
DOI: 10.1016/j.jmb.2012.11.017     Document Type: Article
Times cited : (35)

References (42)
  • 1
    • 22244466130 scopus 로고    scopus 로고
    • The structural biology of type II fatty acid biosynthesis
    • S.W. White, J. Zheng, Y.M. Zhang, and Rock The structural biology of type II fatty acid biosynthesis Annu. Rev. Biochem. 74 2005 791 831
    • (2005) Annu. Rev. Biochem. , vol.74 , pp. 791-831
    • White, S.W.1    Zheng, J.2    Zhang, Y.M.3    Rock4
  • 2
    • 0016840073 scopus 로고
    • Physical properties of membrane lipids: Biological relevance and regulation
    • J.E. Cronan Jr, and E.P. Gelmann Physical properties of membrane lipids: biological relevance and regulation Bacteriol. Rev. 39 1975 232 256
    • (1975) Bacteriol. Rev. , vol.39 , pp. 232-256
    • Cronan Jr., J.E.1    Gelmann, E.P.2
  • 3
    • 0030924134 scopus 로고    scopus 로고
    • Fatty acid biosynthesis in Pseudomonas aeruginosa: Cloning and characterization of the fabAB operon encoding β-hydroxyacyl-acyl carrier protein dehydratase (FabA) and β-ketoacyl-acyl carrier protein synthase i (FabB)
    • T.T. Hoang, and H.P. Schweizer Fatty acid biosynthesis in Pseudomonas aeruginosa: cloning and characterization of the fabAB operon encoding β-hydroxyacyl-acyl carrier protein dehydratase (FabA) and β-ketoacyl-acyl carrier protein synthase I (FabB) J. Bacteriol. 179 1997 5326 5332
    • (1997) J. Bacteriol. , vol.179 , pp. 5326-5332
    • Hoang, T.T.1    Schweizer, H.P.2
  • 4
    • 33645306860 scopus 로고    scopus 로고
    • Two aerobic pathways for the formation of unsaturated fatty acids in Pseudomonas aeruginosa
    • K. Zhu, K.H. Choi, H.P. Schweizer, C.O. Rock, and Y.M. Zhang Two aerobic pathways for the formation of unsaturated fatty acids in Pseudomonas aeruginosa Mol. Microbiol. 60 2006 260 273
    • (2006) Mol. Microbiol. , vol.60 , pp. 260-273
    • Zhu, K.1    Choi, K.H.2    Schweizer, H.P.3    Rock, C.O.4    Zhang, Y.M.5
  • 5
    • 10644295401 scopus 로고    scopus 로고
    • The structure of (3R)-hydroxyacyl-acyl carrier protein dehydratase (FabZ) from Pseudomonas aeruginosa
    • M.S. Kimber, F. Martin, Y. Lu, S. Houston, M. Vedadi, and A. Dharamsi The structure of (3R)-hydroxyacyl-acyl carrier protein dehydratase (FabZ) from Pseudomonas aeruginosa J. Biol. Chem. 279 2004 52593 52602
    • (2004) J. Biol. Chem. , vol.279 , pp. 52593-52602
    • Kimber, M.S.1    Martin, F.2    Lu, Y.3    Houston, S.4    Vedadi, M.5    Dharamsi, A.6
  • 6
    • 24044527131 scopus 로고    scopus 로고
    • Domain swapping between Enterococcus faecalis FabN and FabZ proteins localizes the structural determinants for isomerase activity
    • Y.J. Lu, S.W. White, and C.O. Rock Domain swapping between Enterococcus faecalis FabN and FabZ proteins localizes the structural determinants for isomerase activity J. Biol. Chem. 280 2005 30342 30348
    • (2005) J. Biol. Chem. , vol.280 , pp. 30342-30348
    • Lu, Y.J.1    White, S.W.2    Rock, C.O.3
  • 7
    • 0030584655 scopus 로고    scopus 로고
    • Structure of a dehydratase-isomerase from the bacterial pathway for biosynthesis of unsaturated fatty acids: Two catalytic activities in one active site
    • M. Leesong, B.S. Henderson, J.R. Gillig, J.M. Schwab, and J.L. Smith Structure of a dehydratase-isomerase from the bacterial pathway for biosynthesis of unsaturated fatty acids: two catalytic activities in one active site Structure 4 1996 253 264
    • (1996) Structure , vol.4 , pp. 253-264
    • Leesong, M.1    Henderson, B.S.2    Gillig, J.R.3    Schwab, J.M.4    Smith, J.L.5
  • 8
    • 0034780806 scopus 로고    scopus 로고
    • Bacterial fatty acid biosynthesis: Targets for antibacterial drug discovery
    • J.W. Campbell, and J.E. Cronan Jr. Bacterial fatty acid biosynthesis: targets for antibacterial drug discovery Annu. Rev. Microbiol. 55 2001 305 332
    • (2001) Annu. Rev. Microbiol. , vol.55 , pp. 305-332
    • Campbell, J.W.1    Cronan Jr., J.E.2
  • 9
    • 0036247948 scopus 로고    scopus 로고
    • Inhibitors of fatty acid synthesis as antimicrobial chemotherapeutics
    • R.J. Heath, S.W. White, and C.O. Rock Inhibitors of fatty acid synthesis as antimicrobial chemotherapeutics Appl. Microbiol. Biotechnol. 58 2002 695 703
    • (2002) Appl. Microbiol. Biotechnol. , vol.58 , pp. 695-703
    • Heath, R.J.1    White, S.W.2    Rock, C.O.3
  • 10
    • 80053924657 scopus 로고    scopus 로고
    • Is bacterial fatty acid synthesis a valid target for antibacterial drug discovery?
    • J.B. Parsons, and C.O. Rock Is bacterial fatty acid synthesis a valid target for antibacterial drug discovery? Curr. Opin. Microbiol. 14 2011 544 549
    • (2011) Curr. Opin. Microbiol. , vol.14 , pp. 544-549
    • Parsons, J.B.1    Rock, C.O.2
  • 13
    • 34548232365 scopus 로고    scopus 로고
    • Inference of macromolecular assemblies from crystalline state
    • E. Krissinel, and K. Henrick Inference of macromolecular assemblies from crystalline state J. Mol. Biol. 372 2007 774 797
    • (2007) J. Mol. Biol. , vol.372 , pp. 774-797
    • Krissinel, E.1    Henrick, K.2
  • 14
    • 61949263942 scopus 로고    scopus 로고
    • Type II fatty acid synthesis is not a suitable antibiotic target for Gram-positive pathogens
    • S. Brinster, G. Lamberet, B. Staels, P. Trieu-Cuot, A. Gruss, and C. Poyart Type II fatty acid synthesis is not a suitable antibiotic target for Gram-positive pathogens Nature 458 2009 83 86
    • (2009) Nature , vol.458 , pp. 83-86
    • Brinster, S.1    Lamberet, G.2    Staels, B.3    Trieu-Cuot, P.4    Gruss, A.5    Poyart, C.6
  • 15
    • 65249105921 scopus 로고    scopus 로고
    • Discovering potent inhibitors against the β-hydroxyacyl-acyl carrier protein dehydratase (FabZ) of Helicobacter pylori: Structure-based design, synthesis, bioassay, and crystal structure determination
    • L. He, L. Zhang, X. Liu, X. Li, M. Zheng, and H. Li Discovering potent inhibitors against the β-hydroxyacyl-acyl carrier protein dehydratase (FabZ) of Helicobacter pylori: structure-based design, synthesis, bioassay, and crystal structure determination J. Med. Chem. 52 2009 2465 2481
    • (2009) J. Med. Chem. , vol.52 , pp. 2465-2481
    • He, L.1    Zhang, L.2    Liu, X.3    Li, X.4    Zheng, M.5    Li, H.6
  • 16
    • 84860390428 scopus 로고    scopus 로고
    • Structural basis for the functional and inhibitory mechanisms of β-hydroxyacyl-acyl carrier protein dehydratase (FabZ) of Plasmodium falciparum
    • K. Maity, B.S. Venkata, N. Kapoor, N. Surolia, A. Surolia, and K. Suguna Structural basis for the functional and inhibitory mechanisms of β-hydroxyacyl-acyl carrier protein dehydratase (FabZ) of Plasmodium falciparum J. Struct. Biol. 176 2011 238 249
    • (2011) J. Struct. Biol. , vol.176 , pp. 238-249
    • Maity, K.1    Venkata, B.S.2    Kapoor, N.3    Surolia, N.4    Surolia, A.5    Suguna, K.6
  • 17
    • 41949086428 scopus 로고    scopus 로고
    • Structural basis for catalytic and inhibitory mechanisms of β-hydroxyacyl-acyl carrier protein dehydratase (FabZ)
    • L. Zhang, W. Liu, T. Hu, L. Du, C. Luo, and K. Chen Structural basis for catalytic and inhibitory mechanisms of β-hydroxyacyl-acyl carrier protein dehydratase (FabZ) J. Biol. Chem. 283 2008 5370 5379
    • (2008) J. Biol. Chem. , vol.283 , pp. 5370-5379
    • Zhang, L.1    Liu, W.2    Hu, T.3    Du, L.4    Luo, C.5    Chen, K.6
  • 18
    • 55549098939 scopus 로고    scopus 로고
    • Three flavonoids targeting the β-hydroxyacyl-acyl carrier protein dehydratase from Helicobacter pylori: Crystal structure characterization with enzymatic inhibition assay
    • L. Zhang, Y. Kong, D. Wu, H. Zhang, J. Wu, and J. Chen Three flavonoids targeting the β-hydroxyacyl-acyl carrier protein dehydratase from Helicobacter pylori: crystal structure characterization with enzymatic inhibition assay Protein Sci. 17 2008 1971 1978
    • (2008) Protein Sci. , vol.17 , pp. 1971-1978
    • Zhang, L.1    Kong, Y.2    Wu, D.3    Zhang, H.4    Wu, J.5    Chen, J.6
  • 19
    • 65849155778 scopus 로고    scopus 로고
    • Natural product juglone targets three key enzymes from Helicobacter pylori: Inhibition assay with crystal structure characterization
    • Y.H. Kong, L. Zhang, Z.Y. Yang, C. Han, L.H. Hu, H.L. Jiang, and X. Shen Natural product juglone targets three key enzymes from Helicobacter pylori: inhibition assay with crystal structure characterization Acta Pharmacol. Sin. 29 2008 870 876
    • (2008) Acta Pharmacol. Sin. , vol.29 , pp. 870-876
    • Kong, Y.H.1    Zhang, L.2    Yang, Z.Y.3    Han, C.4    Hu, L.H.5    Jiang, H.L.6    Shen, X.7
  • 20
    • 0001725558 scopus 로고
    • Steric course of the allylic rearrangement catalyzed by β-hydroxydecanoylthioester dehydrase - Mechanistic implications
    • J.M. Schwab, and J.B. Klassen Steric course of the allylic rearrangement catalyzed by β-hydroxydecanoylthioester dehydrase - mechanistic implications J. Am. Chem. Soc. 106 1984 7217 7227
    • (1984) J. Am. Chem. Soc. , vol.106 , pp. 7217-7227
    • Schwab, J.M.1    Klassen, J.B.2
  • 21
    • 29744445671 scopus 로고    scopus 로고
    • Design, synthesis, and evaluation of pharmacological properties of cinnamic derivatives as antiatherogenic agents
    • C. Lapeyre, M. Delomenede, F. Bedos-Belval, H. Duran, A. Negre-Salvayre, and M. Baltas Design, synthesis, and evaluation of pharmacological properties of cinnamic derivatives as antiatherogenic agents J. Med. Chem. 48 2005 8115 8124
    • (2005) J. Med. Chem. , vol.48 , pp. 8115-8124
    • Lapeyre, C.1    Delomenede, M.2    Bedos-Belval, F.3    Duran, H.4    Negre-Salvayre, A.5    Baltas, M.6
  • 22
    • 69449095052 scopus 로고    scopus 로고
    • In vitro precursor-directed synthesis of polyketide analogues with coenzyme a regeneration for the development of antiangiogenic agents
    • M.I. Kim, S.J. Kwon, and J.S. Dordick In vitro precursor-directed synthesis of polyketide analogues with coenzyme a regeneration for the development of antiangiogenic agents Org. Lett. 11 2009 3806 3809
    • (2009) Org. Lett. , vol.11 , pp. 3806-3809
    • Kim, M.I.1    Kwon, S.J.2    Dordick, J.S.3
  • 24
    • 58949085244 scopus 로고    scopus 로고
    • An efficient one-step site-directed deletion, insertion, single and multiple-site plasmid mutagenesis protocol
    • H. Liu, and J.H. Naismith An efficient one-step site-directed deletion, insertion, single and multiple-site plasmid mutagenesis protocol BMC Biotechnol. 8 2008 91
    • (2008) BMC Biotechnol. , vol.8 , pp. 91
    • Liu, H.1    Naismith, J.H.2
  • 25
    • 14844294424 scopus 로고    scopus 로고
    • Protein production by auto-induction in high density shaking cultures
    • F.W. Studier Protein production by auto-induction in high density shaking cultures Protein Expression Purif. 41 2005 207 234
    • (2005) Protein Expression Purif. , vol.41 , pp. 207-234
    • Studier, F.W.1
  • 26
    • 0037463033 scopus 로고    scopus 로고
    • NMR spectroscopy techniques for screening and identifying ligand binding to protein receptors
    • B. Meyer, and T. Peters NMR spectroscopy techniques for screening and identifying ligand binding to protein receptors Angew. Chem. 42 2003 864 890
    • (2003) Angew. Chem. , vol.42 , pp. 864-890
    • Meyer, B.1    Peters, T.2
  • 27
    • 0033789206 scopus 로고    scopus 로고
    • Identification of compounds with binding affinity to proteins via magnetization transfer from bulk water
    • C. Dalvit, P. Pevarello, M. Tato, M. Veronesi, A. Vulpetti, and M. Sundstrom Identification of compounds with binding affinity to proteins via magnetization transfer from bulk water J. Biomol. NMR 18 2000 65 68
    • (2000) J. Biomol. NMR , vol.18 , pp. 65-68
    • Dalvit, C.1    Pevarello, P.2    Tato, M.3    Veronesi, M.4    Vulpetti, A.5    Sundstrom, M.6
  • 28
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Z. Otwinowski, and W. Minor Processing of X-ray diffraction data collected in oscillation mode Methods Enzymol. 276 1997 307 326
    • (1997) Methods Enzymol. , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 29
    • 75649151032 scopus 로고    scopus 로고
    • Xia2: An expert system for macromolecular crystallography data reduction
    • G. Winter Xia2: an expert system for macromolecular crystallography data reduction J. Appl. Crystallogr. 43 2010 186 190
    • (2010) J. Appl. Crystallogr. , vol.43 , pp. 186-190
    • Winter, G.1
  • 30
    • 33645160257 scopus 로고    scopus 로고
    • Automated diffraction image analysis and spot searching for high-throughput crystal screening
    • Z. Zhang, N.K. Sauter, H. van den Bedem, G. Snell, and A.M. Deacon Automated diffraction image analysis and spot searching for high-throughput crystal screening J. Appl. Crystallogr. 39 2006 112 119
    • (2006) J. Appl. Crystallogr. , vol.39 , pp. 112-119
    • Zhang, Z.1    Sauter, N.K.2    Van Den Bedem, H.3    Snell, G.4    Deacon, A.M.5
  • 32
    • 0027879008 scopus 로고
    • Automatic processing of rotation diffraction data from crystals of initially unknown symmetry and cell constants
    • W. Kabsch Automatic processing of rotation diffraction data from crystals of initially unknown symmetry and cell constants J. Appl. Crystallogr. 26 1993 795 800
    • (1993) J. Appl. Crystallogr. , vol.26 , pp. 795-800
    • Kabsch, W.1
  • 34
    • 0000560808 scopus 로고    scopus 로고
    • MOLREP: An automated program for molecular replacement
    • A. Vagin, and A. Teplyakov MOLREP: an automated program for molecular replacement J. Appl. Crystallogr. 30 1997 1022 1025
    • (1997) J. Appl. Crystallogr. , vol.30 , pp. 1022-1025
    • Vagin, A.1    Teplyakov, A.2
  • 42
    • 22244481705 scopus 로고
    • β-Hydroxydecanoyl thioester dehydrase from Escherichia coli
    • L.R. Kass β-Hydroxydecanoyl thioester dehydrase from Escherichia coli Methods Enzymol. 14 1969 73 80
    • (1969) Methods Enzymol. , vol.14 , pp. 73-80
    • Kass, L.R.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.