메뉴 건너뛰기




Volumn 23, Issue 12, 2015, Pages 2213-2223

Structural Basis for Cyclopropanation by a Unique Enoyl-Acyl Carrier Protein Reductase

Author keywords

[No Author keywords available]

Indexed keywords

CARRIER PROTEIN; COENZYME A; CROTONYL COENZYME A; CURACIN A; CURACIN CYCLOPROPANASE; CURACIN ENOYL REDUCTASE; CYCLOPROPANE; ENOYL ACYL CARRIER PROTEIN REDUCTASE; ENOYL REDUCTASE JAMJ; HYDROLASE; JAMAICAMIDE; MEDIUM CHAIN DEHYDROGENASE REDUCTASE; NATURAL PRODUCT; OXIDOREDUCTASE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE; UNCLASSIFIED DRUG; BACTERIAL PROTEIN; CYCLOPROPANE DERIVATIVE; ENOYL ACYL CARRIER PROTEIN REDUCTASE (NADH); THIAZOLE DERIVATIVE;

EID: 84949201589     PISSN: 09692126     EISSN: 18784186     Source Type: Journal    
DOI: 10.1016/j.str.2015.09.013     Document Type: Article
Times cited : (26)

References (51)
  • 2
    • 84871548647 scopus 로고    scopus 로고
    • Insights from the sea: Structural biology of marine polyketide synthases
    • D.L. Akey, J.J. Gehret, D. Khare, and J.L. Smith Insights from the sea: structural biology of marine polyketide synthases Nat. Prod. Rep. 29 2012 1038 1049
    • (2012) Nat. Prod. Rep. , vol.29 , pp. 1038-1049
    • Akey, D.L.1    Gehret, J.J.2    Khare, D.3    Smith, J.L.4
  • 3
    • 84863966874 scopus 로고    scopus 로고
    • Crystal structure and biochemical studies of the trans-acting polyketide enoyl reductase LovC from lovastatin biosynthesis
    • B.D. Ames, C. Nguyen, J. Bruegger, P. Smith, W. Xu, S. Ma, E. Wong, S. Wong, X. Xie, J.W. Li, and et al. Crystal structure and biochemical studies of the trans-acting polyketide enoyl reductase LovC from lovastatin biosynthesis Proc. Natl. Acad. Sci. USA 109 2012 11144 11149
    • (2012) Proc. Natl. Acad. Sci. USA , vol.109 , pp. 11144-11149
    • Ames, B.D.1    Nguyen, C.2    Bruegger, J.3    Smith, P.4    Xu, W.5    Ma, S.6    Wong, E.7    Wong, S.8    Xie, X.9    Li, J.W.10
  • 4
    • 52649133814 scopus 로고    scopus 로고
    • Isoprenoid-like alkylations in polyketide biosynthesis
    • C.T. Calderone Isoprenoid-like alkylations in polyketide biosynthesis Nat. Prod. Rep. 25 2008 845 853
    • (2008) Nat. Prod. Rep. , vol.25 , pp. 845-853
    • Calderone, C.T.1
  • 5
    • 0037151788 scopus 로고    scopus 로고
    • The barbamide biosynthetic gene cluster: A novel marine cyanobacterial system of mixed polyketide synthase (PKS)-non-ribosomal peptide synthetase (NRPS) origin involving an unusual trichloroleucyl starter unit
    • Z. Chang, P. Flatt, W.H. Gerwick, V.A. Nguyen, C.L. Willis, and D.H. Sherman The barbamide biosynthetic gene cluster: a novel marine cyanobacterial system of mixed polyketide synthase (PKS)-non-ribosomal peptide synthetase (NRPS) origin involving an unusual trichloroleucyl starter unit Gene 296 2002 235 247
    • (2002) Gene , vol.296 , pp. 235-247
    • Chang, Z.1    Flatt, P.2    Gerwick, W.H.3    Nguyen, V.A.4    Willis, C.L.5    Sherman, D.H.6
  • 6
    • 4344645019 scopus 로고    scopus 로고
    • Biosynthetic pathway and gene cluster analysis of curacin A, an antitubulin natural product from the tropical marine cyanobacterium Lyngbya majuscula
    • Z. Chang, N. Sitachitta, J.V. Rossi, M.A. Roberts, P.M. Flatt, J. Jia, D.H. Sherman, and W.H. Gerwick Biosynthetic pathway and gene cluster analysis of curacin A, an antitubulin natural product from the tropical marine cyanobacterium Lyngbya majuscula J. Nat. Prod. 67 2004 1356 1367
    • (2004) J. Nat. Prod. , vol.67 , pp. 1356-1367
    • Chang, Z.1    Sitachitta, N.2    Rossi, J.V.3    Roberts, M.A.4    Flatt, P.M.5    Jia, J.6    Sherman, D.H.7    Gerwick, W.H.8
  • 7
    • 33845708150 scopus 로고    scopus 로고
    • New antibiotics from bacterial natural products
    • J. Clardy, M.A. Fischbach, and C.T. Walsh New antibiotics from bacterial natural products Nat. Biotechnol. 24 2006 1541 1550
    • (2006) Nat. Biotechnol. , vol.24 , pp. 1541-1550
    • Clardy, J.1    Fischbach, M.A.2    Walsh, C.T.3
  • 9
    • 84954358425 scopus 로고    scopus 로고
    • Mocr: A novel fusion tag for enhancing solubility that is compatible with structural biology applications
    • J. DelProposto, C.Y. Majmudar, J.L. Smith, and W.C. Brown Mocr: a novel fusion tag for enhancing solubility that is compatible with structural biology applications Protein Expr. Purif. 63 2009 40 49
    • (2009) Protein Expr. Purif. , vol.63 , pp. 40-49
    • DelProposto, J.1    Majmudar, C.Y.2    Smith, J.L.3    Brown, W.C.4
  • 10
    • 3042551455 scopus 로고    scopus 로고
    • Structure and biosynthesis of the jamaicamides, new mixed polyketide-peptide neurotoxins from the marine cyanobacterium Lyngbya majuscula
    • D.J. Edwards, B.L. Marquez, L.M. Nogle, K. McPhail, D.E. Goeger, M.A. Roberts, and W.H. Gerwick Structure and biosynthesis of the jamaicamides, new mixed polyketide-peptide neurotoxins from the marine cyanobacterium Lyngbya majuscula Chem. Biol. 11 2004 817 833
    • (2004) Chem. Biol. , vol.11 , pp. 817-833
    • Edwards, D.J.1    Marquez, B.L.2    Nogle, L.M.3    McPhail, K.4    Goeger, D.E.5    Roberts, M.A.6    Gerwick, W.H.7
  • 13
    • 34547542453 scopus 로고    scopus 로고
    • Synthesis of C5-dicarboxylic acids from C2-units involving crotonyl-CoA carboxylase/reductase: The ethylmalonyl-CoA pathway
    • T.J. Erb, I.A. Berg, V. Brecht, M. Muller, G. Fuchs, and B.E. Alber Synthesis of C5-dicarboxylic acids from C2-units involving crotonyl-CoA carboxylase/reductase: the ethylmalonyl-CoA pathway Proc. Natl. Acad. Sci. USA 104 2007 10631 10636
    • (2007) Proc. Natl. Acad. Sci. USA , vol.104 , pp. 10631-10636
    • Erb, T.J.1    Berg, I.A.2    Brecht, V.3    Muller, M.4    Fuchs, G.5    Alber, B.E.6
  • 14
    • 33748631825 scopus 로고    scopus 로고
    • Assembly-line enzymology for polyketide and nonribosomal peptide antibiotics: Logic, machinery, and mechanisms
    • M.A. Fischbach, and C.T. Walsh Assembly-line enzymology for polyketide and nonribosomal peptide antibiotics: logic, machinery, and mechanisms Chem. Rev. 106 2006 3468 3496
    • (2006) Chem. Rev. , vol.106 , pp. 3468-3496
    • Fischbach, M.A.1    Walsh, C.T.2
  • 15
    • 37248999755 scopus 로고    scopus 로고
    • Crystal structure of the ECH2 catalytic domain of CurF from Lyngbya majuscula. Insights into a decarboxylase involved in polyketide chain beta-branching
    • T.W. Geders, L. Gu, J.C. Mowers, H. Liu, W.H. Gerwick, K. Hakansson, D.H. Sherman, and J.L. Smith Crystal structure of the ECH2 catalytic domain of CurF from Lyngbya majuscula. Insights into a decarboxylase involved in polyketide chain beta-branching J. Biol. Chem. 282 2007 35954 35963
    • (2007) J. Biol. Chem. , vol.282 , pp. 35954-35963
    • Geders, T.W.1    Gu, L.2    Mowers, J.C.3    Liu, H.4    Gerwick, W.H.5    Hakansson, K.6    Sherman, D.H.7    Smith, J.L.8
  • 16
    • 84876928207 scopus 로고    scopus 로고
    • Drug discovery from marine microbes
    • W.H. Gerwick, and A.M. Fenner Drug discovery from marine microbes Microb. Ecol. 65 2013 800 806
    • (2013) Microb. Ecol. , vol.65 , pp. 800-806
    • Gerwick, W.H.1    Fenner, A.M.2
  • 17
    • 84856406381 scopus 로고    scopus 로고
    • Lessons from the past and charting the future of marine natural products drug discovery and chemical biology
    • W.H. Gerwick, and B.S. Moore Lessons from the past and charting the future of marine natural products drug discovery and chemical biology Chem. Biol. 19 2012 85 98
    • (2012) Chem. Biol. , vol.19 , pp. 85-98
    • Gerwick, W.H.1    Moore, B.S.2
  • 18
    • 4744349653 scopus 로고    scopus 로고
    • Structure of three class I human alcohol dehydrogenases complexed with isoenzyme specific formamide inhibitors
    • B.J. Gibbons, and T.D. Hurley Structure of three class I human alcohol dehydrogenases complexed with isoenzyme specific formamide inhibitors Biochemistry 43 2004 12555 12562
    • (2004) Biochemistry , vol.43 , pp. 12555-12562
    • Gibbons, B.J.1    Hurley, T.D.2
  • 19
    • 33746032962 scopus 로고    scopus 로고
    • Metabolic coupling of dehydration and decarboxylation in the curacin A pathway: Functional identification of a mechanistically diverse enzyme pair
    • L. Gu, J. Jia, H. Liu, K. Hakansson, W.H. Gerwick, and D.H. Sherman Metabolic coupling of dehydration and decarboxylation in the curacin A pathway: functional identification of a mechanistically diverse enzyme pair J. Am. Chem. Soc. 128 2006 9014 9015
    • (2006) J. Am. Chem. Soc. , vol.128 , pp. 9014-9015
    • Gu, L.1    Jia, J.2    Liu, H.3    Hakansson, K.4    Gerwick, W.H.5    Sherman, D.H.6
  • 21
    • 77958463670 scopus 로고    scopus 로고
    • Subdivision of the MDR superfamily of medium-chain dehydrogenases/reductases through iterative hidden Markov model refinement
    • J. Hedlund, H. Jornvall, and B. Persson Subdivision of the MDR superfamily of medium-chain dehydrogenases/reductases through iterative hidden Markov model refinement BMC Bioinformatics 11 2010 534
    • (2010) BMC Bioinformatics , vol.11 , pp. 534
    • Hedlund, J.1    Jornvall, H.2    Persson, B.3
  • 22
    • 69249202590 scopus 로고    scopus 로고
    • The biosynthetic logic of polyketide diversity
    • C. Hertweck The biosynthetic logic of polyketide diversity Angew. Chem. Int. Ed. Engl. 48 2009 4688 4716
    • (2009) Angew. Chem. Int. Ed. Engl. , vol.48 , pp. 4688-4716
    • Hertweck, C.1
  • 23
    • 57649229060 scopus 로고    scopus 로고
    • HOLLOW: Generating accurate representations of channel and interior surfaces in molecular structures
    • B.K. Ho, and F. Gruswitz HOLLOW: generating accurate representations of channel and interior surfaces in molecular structures BMC Struct. Biol. 8 2008 49
    • (2008) BMC Struct. Biol. , vol.8 , pp. 49
    • Ho, B.K.1    Gruswitz, F.2
  • 24
  • 25
    • 33750682661 scopus 로고    scopus 로고
    • Crystal structure of anti-configuration of indomethacin and leukotriene B4 12-hydroxydehydrogenase/15-oxo-prostaglandin 13-reductase complex reveals the structural basis of broad spectrum indomethacin efficacy
    • T. Hori, J. Ishijima, T. Yokomizo, H. Ago, T. Shimizu, and M. Miyano Crystal structure of anti-configuration of indomethacin and leukotriene B4 12-hydroxydehydrogenase/15-oxo-prostaglandin 13-reductase complex reveals the structural basis of broad spectrum indomethacin efficacy J. Biochem. 140 2006 457 466
    • (2006) J. Biochem. , vol.140 , pp. 457-466
    • Hori, T.1    Ishijima, J.2    Yokomizo, T.3    Ago, H.4    Shimizu, T.5    Miyano, M.6
  • 26
    • 65449160157 scopus 로고    scopus 로고
    • New tricks from ancient algae: Natural products biosynthesis in marine cyanobacteria
    • A.C. Jones, L. Gu, C.M. Sorrels, D.H. Sherman, and W.H. Gerwick New tricks from ancient algae: natural products biosynthesis in marine cyanobacteria Curr. Opin. Chem. Biol. 13 2009 216 223
    • (2009) Curr. Opin. Chem. Biol. , vol.13 , pp. 216-223
    • Jones, A.C.1    Gu, L.2    Sorrels, C.M.3    Sherman, D.H.4    Gerwick, W.H.5
  • 29
    • 77956942908 scopus 로고    scopus 로고
    • Mutagenesis of a modular polyketide synthase enoylreductase domain reveals insights into catalysis and stereospecificity
    • D.H. Kwan, and P.F. Leadlay Mutagenesis of a modular polyketide synthase enoylreductase domain reveals insights into catalysis and stereospecificity ACS Chem. Biol. 5 2010 829 838
    • (2010) ACS Chem. Biol. , vol.5 , pp. 829-838
    • Kwan, D.H.1    Leadlay, P.F.2
  • 31
    • 80054911951 scopus 로고    scopus 로고
    • LigPlot+: Multiple ligand-protein interaction diagrams for drug discovery
    • R.A. Laskowski, and M.B. Swindells LigPlot+: multiple ligand-protein interaction diagrams for drug discovery J. Chem. Inf. Model 51 2011 2778 2786
    • (2011) J. Chem. Inf. Model , vol.51 , pp. 2778-2786
    • Laskowski, R.A.1    Swindells, M.B.2
  • 33
    • 51149098989 scopus 로고    scopus 로고
    • The crystal structure of a mammalian fatty acid synthase
    • T. Maier, M. Leibundgut, and N. Ban The crystal structure of a mammalian fatty acid synthase Science 321 2008 1315 1322
    • (2008) Science , vol.321 , pp. 1315-1322
    • Maier, T.1    Leibundgut, M.2    Ban, N.3
  • 36
    • 84858308226 scopus 로고    scopus 로고
    • Natural products as sources of new drugs over the 30 years from 1981 to 2010
    • D.J. Newman, and G.M. Cragg Natural products as sources of new drugs over the 30 years from 1981 to 2010 J. Nat. Prod. 75 2012 311 335
    • (2012) J. Nat. Prod. , vol.75 , pp. 311-335
    • Newman, D.J.1    Cragg, G.M.2
  • 37
    • 0036375898 scopus 로고    scopus 로고
    • Medium-chain dehydrogenases/reductases (MDR). Family characterizations including genome comparisons and active site modeling
    • E. Nordling, H. Jornvall, and B. Persson Medium-chain dehydrogenases/reductases (MDR). Family characterizations including genome comparisons and active site modeling Eur. J. Biochem. 269 2002 4267 4276
    • (2002) Eur. J. Biochem. , vol.269 , pp. 4267-4276
    • Nordling, E.1    Jornvall, H.2    Persson, B.3
  • 38
    • 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
  • 39
    • 58149109089 scopus 로고    scopus 로고
    • Medium- and short-chain dehydrogenase/reductase gene and protein families: The MDR superfamily
    • B. Persson, J. Hedlund, and H. Jornvall Medium- and short-chain dehydrogenase/reductase gene and protein families: the MDR superfamily Cell Mol. Life Sci. 65 2008 3879 3894
    • (2008) Cell Mol. Life Sci. , vol.65 , pp. 3879-3894
    • Persson, B.1    Hedlund, J.2    Jornvall, H.3
  • 41
    • 83655163980 scopus 로고    scopus 로고
    • Unusual carbon fixation gives rise to diverse polyketide extender units
    • N. Quade, L. Huo, S. Rachid, D.W. Heinz, and R. Muller Unusual carbon fixation gives rise to diverse polyketide extender units Nat. Chem. Biol. 8 2012 117 124
    • (2012) Nat. Chem. Biol. , vol.8 , pp. 117-124
    • Quade, N.1    Huo, L.2    Rachid, S.3    Heinz, D.W.4    Muller, R.5
  • 44
    • 84949298939 scopus 로고    scopus 로고
    • Schrodinger, LLC The PyMOL Molecular Graphics System, Version 1.3r1 2010 Schrodinger, LLC
    • Schrodinger, LLC The PyMOL Molecular Graphics System, Version 1.3r1 2010 Schrodinger, LLC
  • 45
    • 84950294285 scopus 로고    scopus 로고
    • CHAPTER 18 recent advances in the structural and mechanistic biology of non-haem Fe(II), 2-oxoglutarate and O2-dependent halogenases
    • The Royal Society of Chemistry
    • J.L. Smith, and D. Khare CHAPTER 18 recent advances in the structural and mechanistic biology of non-haem Fe(ii), 2-oxoglutarate and O2-dependent halogenases 2-Oxoglutarate-Dependent Oxygenases 2015 The Royal Society of Chemistry 401 413
    • (2015) 2-Oxoglutarate-Dependent Oxygenases , pp. 401-413
    • Smith, J.L.1    Khare, D.2
  • 46
    • 0036926615 scopus 로고    scopus 로고
    • A new vector for high-throughput, ligation-independent cloning encoding a tobacco etch virus protease cleavage site
    • L. Stols, M. Gu, L. Dieckman, R. Raffen, F.R. Collart, and M.I. Donnelly A new vector for high-throughput, ligation-independent cloning encoding a tobacco etch virus protease cleavage site Protein Expr. Purif. 25 2002 8 15
    • (2002) Protein Expr. Purif. , vol.25 , pp. 8-15
    • Stols, L.1    Gu, M.2    Dieckman, L.3    Raffen, R.4    Collart, F.R.5    Donnelly, M.I.6
  • 47
    • 0002752973 scopus 로고
    • Improved media for growing plasmid and cosmid clones
    • K.D. Tartoff, and C.A. Hobbs Improved media for growing plasmid and cosmid clones Bethesda Res. Labs Focus 9 1987 12
    • (1987) Bethesda Res. Labs Focus , vol.9 , pp. 12
    • Tartoff, K.D.1    Hobbs, C.A.2
  • 48
    • 0028977970 scopus 로고
    • Crystal structure of Escherichia coli QOR quinone oxidoreductase complexed with NADPH
    • J.M. Thorn, J.D. Barton, N.E. Dixon, D.L. Ollis, and K.J. Edwards Crystal structure of Escherichia coli QOR quinone oxidoreductase complexed with NADPH J. Mol. Biol. 249 1995 785 799
    • (1995) J. Mol. Biol. , vol.249 , pp. 785-799
    • Thorn, J.M.1    Barton, J.D.2    Dixon, N.E.3    Ollis, D.L.4    Edwards, K.J.5
  • 49
    • 0033214211 scopus 로고    scopus 로고
    • Biosynthesis of radiolabeled curacin A and its rapid and apparently irreversible binding to the colchicine site of tubulin
    • P. Verdier-Pinard, N. Sitachitta, J.V. Rossi, D.L. Sackett, W.H. Gerwick, and E. Hamel Biosynthesis of radiolabeled curacin A and its rapid and apparently irreversible binding to the colchicine site of tubulin Arch. Biochem. Biophys. 370 1999 51 58
    • (1999) Arch. Biochem. Biophys. , vol.370 , pp. 51-58
    • Verdier-Pinard, P.1    Sitachitta, N.2    Rossi, J.V.3    Sackett, D.L.4    Gerwick, W.H.5    Hamel, E.6
  • 51
    • 84862879901 scopus 로고    scopus 로고
    • Divergence of multimodular polyketide synthases revealed by a didomain structure
    • J. Zheng, D.C. Gay, B. Demeler, M.A. White, and A.T. Keatinge-Clay Divergence of multimodular polyketide synthases revealed by a didomain structure Nat. Chem. Biol. 8 2012 615 621
    • (2012) Nat. Chem. Biol. , vol.8 , pp. 615-621
    • Zheng, J.1    Gay, D.C.2    Demeler, B.3    White, M.A.4    Keatinge-Clay, A.T.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.