메뉴 건너뛰기




Volumn 176, Issue 2, 2011, Pages 238-249

Structural basis for the functional and inhibitory mechanisms of β-hydroxyacyl-acyl carrier protein dehydratase (FabZ) of Plasmodium falciparum

Author keywords

hydroxyacyl ACP dehydratase; Active site inhibitor complex; Fatty acid biosynthesis; Plasmodium falciparum; Substrate binding tunnel; X ray crystallography

Indexed keywords

CARRIER PROTEIN; PROTEIN FABZ; UNCLASSIFIED DRUG;

EID: 84860390428     PISSN: 10478477     EISSN: 10958657     Source Type: Journal    
DOI: 10.1016/j.jsb.2011.07.018     Document Type: Article
Times cited : (27)

References (44)
  • 2
    • 51149120354 scopus 로고    scopus 로고
    • Synthesis and biological evaluation of NAS-21 and NAS-91 analogues as potential inhibitors of the mycobacterial FAS-II dehydratase enzyme Rv0636
    • Bhowruth V., Brown A.K., Besra G.S. Synthesis and biological evaluation of NAS-21 and NAS-91 analogues as potential inhibitors of the mycobacterial FAS-II dehydratase enzyme Rv0636. Microbiology 2008, 154:1866-1875.
    • (2008) Microbiology , vol.154 , pp. 1866-1875
    • Bhowruth, V.1    Brown, A.K.2    Besra, G.S.3
  • 3
    • 0014199095 scopus 로고
    • Beta-hydroxydecanoyl thioester dehydrase II. Mode of action
    • Brock D.J., Kass L.R., Bloch K. Beta-hydroxydecanoyl thioester dehydrase II. Mode of action. J. Biol. Chem. 1967, 242:4432-4440.
    • (1967) J. Biol. Chem. , vol.242 , pp. 4432-4440
    • Brock, D.J.1    Kass, L.R.2    Bloch, K.3
  • 4
    • 0001679473 scopus 로고    scopus 로고
    • ALIGN: a program to superimpose protein coordinates accounting for insertions and deletions
    • Cohen G.H. ALIGN: a program to superimpose protein coordinates accounting for insertions and deletions. J. Appl. Crystallogr. 1997, 30:1160-1161.
    • (1997) J. Appl. Crystallogr. , vol.30 , pp. 1160-1161
    • Cohen, G.H.1
  • 5
    • 0028103275 scopus 로고
    • Collaborative Computational Project Number 4. The CCP4 suite: programs for protein crystallography. Acta Crystallogr. D50
    • Collaborative Computational Project Number 4, 1994. The CCP4 suite: programs for protein crystallography. Acta Crystallogr. D50, 760-763.
    • (1994) , pp. 760-763
  • 6
    • 13244267005 scopus 로고    scopus 로고
    • The Hotdog fold: wrapping up a superfamily of thioesterases and dehydratases
    • Dillon S.C., Bateman A. The Hotdog fold: wrapping up a superfamily of thioesterases and dehydratases. BMC Bioinformatics 2004, 5:109.
    • (2004) BMC Bioinformatics , vol.5 , pp. 109
    • Dillon, S.C.1    Bateman, A.2
  • 8
    • 49149147973 scopus 로고
    • Interactive partial equalization of orbital electronegativity - a rapid access to atomic charges
    • Gasteiger J., Marsili M. Interactive partial equalization of orbital electronegativity - a rapid access to atomic charges. Tetrahedron 1980, 36:3219-3228.
    • (1980) Tetrahedron , vol.36 , pp. 3219-3228
    • Gasteiger, J.1    Marsili, M.2
  • 9
    • 0043123208 scopus 로고    scopus 로고
    • ESPript/ENDscript: extracting and rendering sequence and 3D information from atomic structures of proteins
    • Gouet P., Robert X., Courcelle E. ESPript/ENDscript: extracting and rendering sequence and 3D information from atomic structures of proteins. Nucleic Acids Res. 2003, 31:3320-3323.
    • (2003) Nucleic Acids Res. , vol.31 , pp. 3320-3323
    • Gouet, P.1    Robert, X.2    Courcelle, E.3
  • 10
    • 40549088222 scopus 로고    scopus 로고
    • Antimycobacterial activity and mechanism of action of NAS-91 antimicrob
    • Gratraud P., Surolia N., Besra G.S., Surolia A., Kremer L. Antimycobacterial activity and mechanism of action of NAS-91 antimicrob. Agents Chemother. 2008, 52:1162-1166.
    • (2008) Agents Chemother. , vol.52 , pp. 1162-1166
    • Gratraud, P.1    Surolia, N.2    Besra, G.S.3    Surolia, A.4    Kremer, L.5
  • 11
    • 65249105921 scopus 로고    scopus 로고
    • Discovering potent inhibitors against the beta-hydroxyacyl-acyl carrier protein dehydratase (FabZ) of Helicobacter pylori: structure-based design, synthesis, bioassay, and crystal structure determination
    • He L., Zhang L., Liu X., Li X., Zheng M., et al. Discovering potent inhibitors against the beta-hydroxyacyl-acyl carrier protein dehydratase (FabZ) of Helicobacter pylori: structure-based design, synthesis, bioassay, and crystal structure determination. J. Med. Chem. 2009, 52:2465-2481.
    • (2009) J. Med. Chem. , vol.52 , pp. 2465-2481
    • He, L.1    Zhang, L.2    Liu, X.3    Li, X.4    Zheng, M.5
  • 12
    • 0029926496 scopus 로고    scopus 로고
    • Roles of the FabA and FabZ beta-hydroxyacyl-acyl carrier protein dehydratases in Escherichia coli fatty acid biosynthesis
    • Heath R.J., Rock C.O. Roles of the FabA and FabZ beta-hydroxyacyl-acyl carrier protein dehydratases in Escherichia coli fatty acid biosynthesis. J. Biol. Chem. 1996, 271:27795-27801.
    • (1996) J. Biol. Chem. , vol.271 , pp. 27795-27801
    • Heath, R.J.1    Rock, C.O.2
  • 13
    • 57649229060 scopus 로고    scopus 로고
    • HOLLOW: generating accurate representations of channel and interior surfaces in molecular structures
    • Ho B.K., Gruswitz F. HOLLOW: generating accurate representations of channel and interior surfaces in molecular structures. BMC Struct. Biol. 2008, 8:49.
    • (2008) BMC Struct. Biol. , vol.8 , pp. 49
    • Ho, B.K.1    Gruswitz, F.2
  • 14
    • 0030590426 scopus 로고    scopus 로고
    • How good is fluorine as a hydrogen bond acceptor?
    • Howard J.A.K., Hoy V.J., O'Hagan D., Smith G.T. How good is fluorine as a hydrogen bond acceptor?. Tetrahedron 1996, 52:12613-12622.
    • (1996) Tetrahedron , vol.52 , pp. 12613-12622
    • Howard, J.A.K.1    Hoy, V.J.2    O'Hagan, D.3    Smith, G.T.4
  • 16
    • 33947716119 scopus 로고    scopus 로고
    • A semiempirical free energy force field with charge-based desolvation
    • Huey R., Morris G.M., Olson A.J., Goodsell D.S. A semiempirical free energy force field with charge-based desolvation. J. Comput. Chem. 2007, 28:1145-1152.
    • (2007) J. Comput. Chem. , vol.28 , pp. 1145-1152
    • Huey, R.1    Morris, G.M.2    Olson, A.J.3    Goodsell, D.S.4
  • 17
    • 10644295401 scopus 로고    scopus 로고
    • The structure of (3R)-hydroxyacyl-acyl carrier protein dehydratase (FabZ) from Pseudomonas aeruginosa
    • Kimber M.S., Martin F., Lu Y., Houston S., Vedadi M., et al. The structure of (3R)-hydroxyacyl-acyl carrier protein dehydratase (FabZ) from Pseudomonas aeruginosa. J. Biol. Chem. 2004, 279:52593-52602.
    • (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
  • 18
    • 60349119365 scopus 로고    scopus 로고
    • Campylobacter jejuni fatty acid synthase II: structural and functional analysis of beta-hydroxyacyl-ACP dehydratase (FabZ)
    • Kirkpatrick A.S., Yokoyama T., Choi K.J., Yeo H.J. Campylobacter jejuni fatty acid synthase II: structural and functional analysis of beta-hydroxyacyl-ACP dehydratase (FabZ). Biochem. Biophys. Res. Commun. 2009, 380:407-412.
    • (2009) Biochem. Biophys. Res. Commun. , vol.380 , pp. 407-412
    • Kirkpatrick, A.S.1    Yokoyama, T.2    Choi, K.J.3    Yeo, H.J.4
  • 19
    • 22544476228 scopus 로고    scopus 로고
    • The crystal structure of PfFabZ, the unique beta-hydroxyacyl-ACP dehydratase involved in fatty acid biosynthesis of Plasmodium falciparum
    • Kostrewa D., Winkler F.K., Folkers G., Scapozza L., Perozzo R. The crystal structure of PfFabZ, the unique beta-hydroxyacyl-ACP dehydratase involved in fatty acid biosynthesis of Plasmodium falciparum. Protein Sci. 2005, 14:1570-1580.
    • (2005) Protein Sci. , vol.14 , pp. 1570-1580
    • Kostrewa, D.1    Winkler, F.K.2    Folkers, G.3    Scapozza, L.4    Perozzo, R.5
  • 20
    • 84860393504 scopus 로고    scopus 로고
    • Biochemical and molecular insights into β-hydroxyacyl-acyl carrier protein dehydratase (FabZ) from Plasmodium falciparum
    • Ph.D. Thesis, Indian Institute of Science.
    • Kumar, S., 2006. Biochemical and molecular insights into β-hydroxyacyl-acyl carrier protein dehydratase (FabZ) from Plasmodium falciparum. Ph.D. Thesis, Indian Institute of Science.
    • (2006)
    • Kumar, S.1
  • 21
  • 22
    • 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
    • Leesong M., Henderson B.S., Gillig J.R., Schwab J.M., Smith J.L. Structure of a dehydratase-isomerase from the bacterial pathway for biosynthesis of unsaturated fatty acids: two catalytic activities in one active site. Structure 1996, 4:253-264.
    • (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
  • 23
    • 57049083416 scopus 로고    scopus 로고
    • The multienzyme architecture of eukaryotic fatty acid synthases
    • Leibundgut M., Maier T., Jenni S., Ban N. The multienzyme architecture of eukaryotic fatty acid synthases. Curr. Opin. Struct. Biol. 2008, 18:714-725.
    • (2008) Curr. Opin. Struct. Biol. , vol.18 , pp. 714-725
    • Leibundgut, M.1    Maier, T.2    Jenni, S.3    Ban, N.4
  • 24
    • 0003076963 scopus 로고
    • Recent changes to the MOSFLM package for processing film and image plate data. Jnt. CCP4/ESF-EACBM Newsl. Protein Crystallogr.
    • Leslie, A.G.W., 1992. Recent changes to the MOSFLM package for processing film and image plate data. Jnt. CCP4/ESF-EACBM Newsl. Protein Crystallogr. 26, 27-33.
    • (1992) , vol.26 , pp. 27-33
    • Leslie, A.G.W.1
  • 25
    • 77953581267 scopus 로고    scopus 로고
    • X-ray crystallographic analysis of the complexes of enoyl acyl carrier protein reductase of Plasmodium falciparum with triclosan variants to elucidate the importance of different functional groups in enzyme inhibition
    • Maity K., Bhargav S.P., Sankaran B., Surolia N., Surolia A., et al. X-ray crystallographic analysis of the complexes of enoyl acyl carrier protein reductase of Plasmodium falciparum with triclosan variants to elucidate the importance of different functional groups in enzyme inhibition. IUBMB Life 2010, 62:467-476.
    • (2010) IUBMB Life , vol.62 , pp. 467-476
    • Maity, K.1    Bhargav, S.P.2    Sankaran, B.3    Surolia, N.4    Surolia, A.5
  • 26
    • 0037160079 scopus 로고    scopus 로고
    • A new mechanism for anaerobic unsaturated fatty acid formation in Streptococcus pneumoniae
    • Marrakchi H., Choi K.H., Rock C.O. A new mechanism for anaerobic unsaturated fatty acid formation in Streptococcus pneumoniae. J. Biol. Chem. 2002, 277:44809-44816.
    • (2002) J. Biol. Chem. , vol.277 , pp. 44809-44816
    • Marrakchi, H.1    Choi, K.H.2    Rock, C.O.3
  • 27
    • 0026332547 scopus 로고
    • Electrostatic effects in proteins: comparison of dielectric and charge models
    • Mehler E.L., Solmajer T. Electrostatic effects in proteins: comparison of dielectric and charge models. Protein Eng. 1991, 4:903-910.
    • (1991) Protein Eng. , vol.4 , pp. 903-910
    • Mehler, E.L.1    Solmajer, T.2
  • 28
    • 0030924992 scopus 로고    scopus 로고
    • Refinement of macromolecular structures by the maximum-likelihood method
    • Murshudov G.N., Vagin A.A., Dodson E.J. Refinement of macromolecular structures by the maximum-likelihood method. Acta Crystallogr. 1997, D53:240-255.
    • (1997) Acta Crystallogr. , vol.D53 , pp. 240-255
    • Murshudov, G.N.1    Vagin, A.A.2    Dodson, E.J.3
  • 29
    • 17844404530 scopus 로고    scopus 로고
    • Amodiaquine alone, amodiaquine+sulfadoxine-pyrimethamine, amodiaquine+artesunate, and artemether-lumefantrine for outpatient treatment of malaria in Tanzanian children: a four-arm randomised effectiveness trial
    • Mutabingwa T.K., Anthony D., Heller A., Hallett R., Ahmed J., et al. Amodiaquine alone, amodiaquine+sulfadoxine-pyrimethamine, amodiaquine+artesunate, and artemether-lumefantrine for outpatient treatment of malaria in Tanzanian children: a four-arm randomised effectiveness trial. Lancet 2005, 365:1474-1480.
    • (2005) Lancet , vol.365 , pp. 1474-1480
    • Mutabingwa, T.K.1    Anthony, D.2    Heller, A.3    Hallett, R.4    Ahmed, J.5
  • 30
    • 67649535200 scopus 로고    scopus 로고
    • Analysis of proteins with the 'hot dog' fold: prediction of function and identification of catalytic residues of hypothetical proteins
    • Pidugu L.S., Maity K., Ramaswamy K., Surolia N., Suguna K. Analysis of proteins with the 'hot dog' fold: prediction of function and identification of catalytic residues of hypothetical proteins. BMC Struct. Biol. 2009, 9:37.
    • (2009) BMC Struct. Biol. , vol.9 , pp. 37
    • Pidugu, L.S.1    Maity, K.2    Ramaswamy, K.3    Surolia, N.4    Suguna, K.5
  • 31
    • 0030581109 scopus 로고    scopus 로고
    • Escherichia coli as a model for the regulation of dissociable (type II) fatty acid biosynthesis
    • Rock C.O., Cronan J.E. Escherichia coli as a model for the regulation of dissociable (type II) fatty acid biosynthesis. Biochim. Biophys. Acta 1996, 1302:1-16.
    • (1996) Biochim. Biophys. Acta , vol.1302 , pp. 1-16
    • Rock, C.O.1    Cronan, J.E.2
  • 32
    • 0242580787 scopus 로고    scopus 로고
    • Identification, characterization, and inhibition of Plasmodium falciparum beta-hydroxyacyl-acyl carrier protein dehydratase (FabZ)
    • Sharma S.K., Kapoor M., Ramya T.N., Kumar S., Kumar G., et al. Identification, characterization, and inhibition of Plasmodium falciparum beta-hydroxyacyl-acyl carrier protein dehydratase (FabZ). J. Biol. Chem. 2003, 278:45661-45671.
    • (2003) J. Biol. Chem. , vol.278 , pp. 45661-45671
    • Sharma, S.K.1    Kapoor, M.2    Ramya, T.N.3    Kumar, S.4    Kumar, G.5
  • 33
    • 33847401359 scopus 로고    scopus 로고
    • Green tea catechins potentiate triclosan binding to enoyl-ACP reductase from Plasmodium falciparum (PfENR)
    • Sharma S.K., Parasuraman P., Kumar G., Surolia N., Surolia A. Green tea catechins potentiate triclosan binding to enoyl-ACP reductase from Plasmodium falciparum (PfENR). J. Med. Chem. 2007, 50:765-775.
    • (2007) J. Med. Chem. , vol.50 , pp. 765-775
    • Sharma, S.K.1    Parasuraman, P.2    Kumar, G.3    Surolia, N.4    Surolia, A.5
  • 34
    • 70350752494 scopus 로고    scopus 로고
    • Triclosan inhibit the growth of the late liver-stage of Plasmodium
    • Singh A.P., Surolia N., Surolia A. Triclosan inhibit the growth of the late liver-stage of Plasmodium. IUBMB Life 2009, 61:923-928.
    • (2009) IUBMB Life , vol.61 , pp. 923-928
    • Singh, A.P.1    Surolia, N.2    Surolia, A.3
  • 35
  • 37
    • 0035126479 scopus 로고    scopus 로고
    • Triclosan offers protection against blood stages of malaria by inhibiting enoyl-ACP reductase of Plasmodium falciparum
    • Surolia N., Surolia A. Triclosan offers protection against blood stages of malaria by inhibiting enoyl-ACP reductase of Plasmodium falciparum. Nat. Med. 2001, 7:167-173.
    • (2001) Nat. Med. , vol.7 , pp. 167-173
    • Surolia, N.1    Surolia, A.2
  • 38
    • 33646203969 scopus 로고    scopus 로고
    • Crystal structure of dimeric FabZ of Plasmodium falciparum reveals conformational switching to active hexamers by peptide flips
    • Swarnamukhi P.L., Sharma S.K., Bajaj P., Surolia N., Surolia A., et al. Crystal structure of dimeric FabZ of Plasmodium falciparum reveals conformational switching to active hexamers by peptide flips. FEBS Lett. 2006, 580:2653-2660.
    • (2006) FEBS Lett. , vol.580 , pp. 2653-2660
    • Swarnamukhi, P.L.1    Sharma, S.K.2    Bajaj, P.3    Surolia, N.4    Surolia, A.5
  • 39
    • 33744819176 scopus 로고    scopus 로고
    • Inhibition of Plasmodium falciparum fatty acid biosynthesis: evaluation of FabG, FabZ, and FabI as drug targets for flavonoids
    • Tasdemir D., Lack G., Brun R., Ruedi P., Scapozza L., et al. Inhibition of Plasmodium falciparum fatty acid biosynthesis: evaluation of FabG, FabZ, and FabI as drug targets for flavonoids. J. Med. Chem. 2006, 49:3345-3353.
    • (2006) J. Med. Chem. , vol.49 , pp. 3345-3353
    • Tasdemir, D.1    Lack, G.2    Brun, R.3    Ruedi, P.4    Scapozza, L.5
  • 40
    • 0027968068 scopus 로고
    • CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice
    • Thompson J.D., Higgins D.G., Gibson T.J. CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice. Nucleic Acids Res. 1994, 22:4673-4680.
    • (1994) Nucleic Acids Res. , vol.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3
  • 41
    • 14744295748 scopus 로고    scopus 로고
    • The plastid-derived organelle of protozoan human parasites as a target of established and emerging drugs
    • Wiesner J., Seeber F. The plastid-derived organelle of protozoan human parasites as a target of established and emerging drugs. Expert Opin. Ther. Targets 2005, 9:23-44.
    • (2005) Expert Opin. Ther. Targets , vol.9 , pp. 23-44
    • Wiesner, J.1    Seeber, F.2
  • 42
    • 77249123257 scopus 로고    scopus 로고
    • World Health Organization
    • World Health Organization, Geneva, Switzerland.
    • World Health Organization, 2008. WHO World Malaria Report. World Health Organization, Geneva, Switzerland.
    • (2008) WHO World Malaria Report
  • 43
    • 55549098939 scopus 로고    scopus 로고
    • Three flavonoids targeting the beta-hydroxyacyl-acyl carrier protein dehydratase from Helicobacter pylori: crystal structure characterization with enzymatic inhibition assay
    • Zhang L., Kong Y., Wu D., Zhang H., Wu J., et al. Three flavonoids targeting the beta-hydroxyacyl-acyl carrier protein dehydratase from Helicobacter pylori: crystal structure characterization with enzymatic inhibition assay. Protein Sci. 2008, 17:1971-1978.
    • (2008) Protein Sci. , vol.17 , pp. 1971-1978
    • Zhang, L.1    Kong, Y.2    Wu, D.3    Zhang, H.4    Wu, J.5
  • 44
    • 41949086428 scopus 로고    scopus 로고
    • Structural basis for catalytic and inhibitory mechanisms of beta-hydroxyacyl-acyl carrier protein dehydratase (FabZ)
    • Zhang L., Liu W., Hu T., Du L., Luo C., et al. Structural basis for catalytic and inhibitory mechanisms of beta-hydroxyacyl-acyl carrier protein dehydratase (FabZ). J. Biol. Chem. 2008, 283:5370-5379.
    • (2008) J. Biol. Chem. , vol.283 , pp. 5370-5379
    • Zhang, L.1    Liu, W.2    Hu, T.3    Du, L.4    Luo, C.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.