메뉴 건너뛰기




Volumn 446, Issue 3, 2012, Pages 395-404

Crystal structure of the dopamine N-acetyltransferase-acetyl-CoA complex provides insights into the catalytic mechanism

Author keywords

Arylalkylamine N acetyltransferase (AANAT); Catalytic triad; Dopamine N acetyltransferase (Dat); Melatonin; Single wavelength anomalous diffraction

Indexed keywords

ACETYL COENZYME A; ACYLTRANSFERASE; DOPAMINE N ACETYLTRANSFERASE ACETYL COENZYME A; GLUTAMINE; SELENIUM; SERINE; UNCLASSIFIED DRUG;

EID: 84865587472     PISSN: 02646021     EISSN: 14708728     Source Type: Journal    
DOI: 10.1042/BJ20120520     Document Type: Article
Times cited : (32)

References (50)
  • 3
    • 0001925353 scopus 로고    scopus 로고
    • Ubiquitous melatonin. Presence and effects in unicells, plants and animals
    • Hardeland, R. and Fuhrberg, B. (1996) Ubiquitous melatonin. Presence and effects in unicells, plants and animals. Trends Comp. Biochem. Physiol. 2, 25-45
    • (1996) Trends Comp. Biochem. Physiol. , vol.2 , pp. 25-45
    • Hardeland, R.1    Fuhrberg, B.2
  • 4
    • 0023953560 scopus 로고
    • Melatonin biosynthesis in Drosophila: Its nature and its effects
    • Finocchiaro, L., Callebert, J., Launay, J. M. and Jallon, J. M. (1988) Melatonin biosynthesis in Drosophila: its nature and its effects. J. Neurochem. 50, 382-387
    • (1988) J. Neurochem. , vol.50 , pp. 382-387
    • Finocchiaro, L.1    Callebert, J.2    Launay, J.M.3    Jallon, J.M.4
  • 5
    • 0027199792 scopus 로고
    • Melatonin: Presence and formation in invertebrates
    • Vivien-Roels, B. and Pévet, P. (1993) Melatonin: presence and formation in invertebrates. Experientia 49, 642-647
    • (1993) Experientia , vol.49 , pp. 642-647
    • Vivien-Roels, B.1    Pévet, P.2
  • 6
    • 0027210003 scopus 로고
    • The melatonin rhythm: Both a clock and a calendar
    • Reiter, R. J. (1993) The melatonin rhythm: both a clock and a calendar. Experientia 49, 654-664
    • (1993) Experientia , vol.49 , pp. 654-664
    • Reiter, R.J.1
  • 7
    • 0023515281 scopus 로고
    • The genetics of biogenic amine metabolism, sclerotization, and melanization in Drosophila melanogaster
    • Wright, T. R. (1987) The genetics of biogenic amine metabolism, sclerotization, and melanization in Drosophila melanogaster. Adv. Genet. 24, 127-222
    • (1987) Adv. Genet. , vol.24 , pp. 127-222
    • Wright, T.R.1
  • 9
    • 0003850747 scopus 로고
    • Enzymatic N-acetylation of indolealkylamines by brain homogenates of the honeybee, Apis mellifera
    • Evans, P. and Michaelfox, P. (1975) Enzymatic N-acetylation of indolealkylamines by brain homogenates of the honeybee, Apis mellifera. J. Insect Physiol. 21, 343-353
    • (1975) J. Insect Physiol. , vol.21 , pp. 343-353
    • Evans, P.1    Michaelfox, P.2
  • 10
    • 0016801248 scopus 로고
    • Catabolism of tryptamine by cockroach head enzyme preparation
    • Nishimura, K. (1975) Catabolism of tryptamine by cockroach head enzyme preparation. Pestic. Biochem. Physiol. 5, 557-565
    • (1975) Pestic. Biochem. Physiol. , vol.5 , pp. 557-565
    • Nishimura, K.1
  • 11
    • 0013889993 scopus 로고
    • Biosynthesis of catecholamines in insects
    • Sekeris, C. E. and Karlson, P. (1966) Biosynthesis of catecholamines in insects. Pharmacol. Rev. 18, 89-94
    • (1966) Pharmacol. Rev. , vol.18 , pp. 89-94
    • Sekeris, C.E.1    Karlson, P.2
  • 12
    • 0033646107 scopus 로고    scopus 로고
    • Purification, cloning, and characterization of a second arylalkylamine N-acetyltransferase from Drosophila melanogaster
    • Amherd, R., Hintermann, E., Walz, D., Affolter, M. and Meyer, U. A. (2000) Purification, cloning, and characterization of a second arylalkylamine N-acetyltransferase from Drosophila melanogaster. DNA Cell Biol. 19, 697-705
    • (2000) DNA Cell Biol. , vol.19 , pp. 697-705
    • Amherd, R.1    Hintermann, E.2    Walz, D.3    Affolter, M.4    Meyer, U.A.5
  • 14
    • 0030954208 scopus 로고    scopus 로고
    • GCN5-related histone N-acetyltransferases belong to a diverse superfamily that includes the yeast SPT10 protein
    • DOI 10.1016/S0968-0004(97)01034-7, PII S0968000497010347
    • Neuwald, A. F. and Landsman, D. (1997) GCN5-related histone N-acetyltransferases belong to a diverse superfamily that includes the yeast SPT10 protein. Trends Biochem. Sci. 22, 154-155 (Pubitemid 27199313)
    • (1997) Trends in Biochemical Sciences , vol.22 , Issue.5 , pp. 154-155
    • Neuwald, A.F.1    Landsman, D.2
  • 15
    • 0033010021 scopus 로고    scopus 로고
    • Melatonin biosynthesis: The structure of serotonin N-acetyltransferase at 2.5 A resolution suggests a catalytic mechanism
    • DOI 10.1016/S1097-2765(00)80171-9
    • Hickman, A. B., Klein, D. C. and Dyda, F. (1999) Melatonin biosynthesis: the structure of serotonin N-acetyltransferase at 2.5 Å resolution suggests a catalytic mechanism. Mol. Cell 3, 23-32 (Pubitemid 29292474)
    • (1999) Molecular Cell , vol.3 , Issue.1 , pp. 23-32
    • Hickman, A.B.1    Klein, D.C.2    Dyda, F.3
  • 16
    • 0033617457 scopus 로고    scopus 로고
    • The structural basis of ordered substrate binding by serotonin N-acetyltransferase: Enzyme complex at 1.8 Å resolution with a bisubstrate analog
    • Hickman, A. B., Namboodiri, M. A., Klein, D. C. and Dyda, F. (1999) The structural basis of ordered substrate binding by serotonin N-acetyltransferase: enzyme complex at 1.8 Å resolution with a bisubstrate analog. Cell 97, 361-369
    • (1999) Cell , vol.97 , pp. 361-369
    • Hickman, A.B.1    Namboodiri, M.A.2    Klein, D.C.3    Dyda, F.4
  • 17
    • 0037124069 scopus 로고    scopus 로고
    • Investigation of the roles of catalytic residues in serotonin N-acetyltransferase
    • DOI 10.1074/jbc.M200595200
    • Scheibner, K. A., De Angelis, J., Burley, S. K. and Cole, P. A. (2002) Investigation of the roles of catalytic residues in serotonin N-acetyltransferase. J. Biol. Chem. 277, 18118-18126 (Pubitemid 34967627)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.20 , pp. 18118-18126
    • Scheibner, K.A.1    De Angelis, J.2    Burley, S.K.3    Cole, P.A.4
  • 18
    • 0026095584 scopus 로고
    • Determination of macromolecular structures from anomalous diffraction of synchrotron radiation
    • Hendrickson, W. A. (1991) Determination of macromolecular structures from anomalous diffraction of synchrotron radiation. Science 254, 51-58
    • (1991) Science , vol.254 , pp. 51-58
    • Hendrickson, W.A.1
  • 19
  • 20
    • 0031045585 scopus 로고    scopus 로고
    • Preparation of selenomethionyl proteins for phase determination
    • Doublie, S. (1997) Preparation of selenomethionyl proteins for phase determination. Methods Enzymol. 276, 523-530
    • (1997) Methods Enzymol. , vol.276 , pp. 523-530
    • Doublie, S.1
  • 22
    • 77950793231 scopus 로고    scopus 로고
    • Experimental phasing with SHELXC/D/E: Combining chain tracing with density modification
    • Sheldrick, G. M. (2010) Experimental phasing with SHELXC/D/E: combining chain tracing with density modification. Acta Crystallogr., Sect. D: Biol. Crystallogr. 66, 479-485
    • (2010) Acta Crystallogr., Sect. D: Biol. Crystallogr. , vol.66 , pp. 479-485
    • Sheldrick, G.M.1
  • 23
    • 47749084660 scopus 로고    scopus 로고
    • Pattern-recognition-based detection of planar objects in three-dimensional electron-density maps
    • DOI 10.1107/S0907444908014327, PII S0907444908014327
    • Hattne, J. and Lamzin, V. S. (2008) Pattern-recognition-based detection of planar objects in three-dimensional electron-density maps. Acta Crystallogr., Sect. D: Biol. Crystallogr. 64, 834-842 (Pubitemid 352032287)
    • (2008) Acta Crystallographica Section D: Biological Crystallography , vol.64 , Issue.8 , pp. 834-842
    • Hattne, J.1    Lamzin, V.S.2
  • 26
    • 0027169515 scopus 로고
    • Main-chain bond lengths and bond angles in protein structures
    • DOI 10.1006/jmbi.1993.1351
    • Laskowski, R. A., Moss, D. S. and Thornton, J. M. (1993) Main-chain bond lengths and bond angles in protein structures. J. Mol. Biol. 231, 1049-1067 (Pubitemid 23209879)
    • (1993) Journal of Molecular Biology , vol.231 , Issue.4 , pp. 1049-1067
    • Laskowski, R.A.1    Moss, D.S.2    Thornton, J.M.3
  • 28
    • 0032514895 scopus 로고    scopus 로고
    • Indoleamine analogs as probes of the substrate selectivity and catalytic mechanism of serotonin N-acetyltransferase
    • DOI 10.1074/jbc.273.46.30321
    • Khalil, E. M., De Angelis, J. and Cole, P. A. (1998) Indoleamine analogs as probes of the substrate selectivity and catalytic mechanism of serotonin N-acetyltransferase. J. Biol. Chem. 273, 30321-30327 (Pubitemid 28545501)
    • (1998) Journal of Biological Chemistry , vol.273 , Issue.46 , pp. 30321-30327
    • Khalil, E.M.1    De Angelis, J.2    Cole, P.A.3
  • 29
    • 0031552362 scopus 로고    scopus 로고
    • Development and validation of a genetic algorithm for flexible docking
    • DOI 10.1006/jmbi.1996.0897
    • Jones, G., Willett, P., Glen, R. C., Leach, A. R. and Taylor, R. (1997) Development and validation of a genetic algorithm for flexible docking. J. Mol. Biol. 267, 727-748 (Pubitemid 27170693)
    • (1997) Journal of Molecular Biology , vol.267 , Issue.3 , pp. 727-748
    • Jones, G.1    Willett, P.2    Glen, R.C.3    Leach, A.R.4    Taylor, R.5
  • 30
    • 0028922586 scopus 로고
    • LIGPLOT: A program to generate schematic diagrams of protein-ligand interactions
    • Wallace, A. C., Laskowski, R. A. and Thornton, J. M. (1995) LIGPLOT: a program to generate schematic diagrams of protein-ligand interactions. Protein Eng. 8, 127-134
    • (1995) Protein Eng. , vol.8 , pp. 127-134
    • Wallace, A.C.1    Laskowski, R.A.2    Thornton, J.M.3
  • 31
    • 3242885293 scopus 로고    scopus 로고
    • The PredictProtein server
    • DOI 10.1093/nar/gkh377
    • Rost, B., Yachdav, G. and Liu, J. (2004) The PredictProtein server. Nucleic Acids Res. 32, W321-W326 (Pubitemid 39004075)
    • (2004) Nucleic Acids Research , vol.32 , Issue.WEB SERVER ISS.
    • Rost, B.1    Yachdav, G.2    Liu, J.3
  • 32
    • 67849101183 scopus 로고    scopus 로고
    • ISARST: An integrated SARST web server for rapid protein structural similarity searches
    • Lo, W. C., Lee, C. Y., Lee, C. C. and Lyu, P. C. (2009) iSARST: an integrated SARST web server for rapid protein structural similarity searches. Nucleic Acids Res. 37, W545-W551
    • (2009) Nucleic Acids Res. , vol.37
    • Lo, W.C.1    Lee, C.Y.2    Lee, C.C.3    Lyu, P.C.4
  • 33
    • 0037474532 scopus 로고    scopus 로고
    • Crystal structure of tabtoxin resistance protein complexed with acetyl coenzyme A reveals the mechanism for β-lactam acetylation
    • DOI 10.1016/S0022-2836(02)01284-6
    • He, H., Ding, Y., Bartlam, M., Sun, F., Le, Y., Qin, X., Tang, H., Zhang, R., Joachimiak, A. and Liu, J. (2003) Crystal structure of tabtoxin resistance protein complexed with acetyl coenzyme A reveals the mechanism for β-lactam acetylation. J. Mol. Biol. 325, 1019-1030 (Pubitemid 36263409)
    • (2003) Journal of Molecular Biology , vol.325 , Issue.5 , pp. 1019-1030
    • He, H.1    Ding, Y.2    Bartlam, M.3    Sun, F.4    Le, Y.5    Qin, X.6    Tang, H.7    Zhang, R.8    Joachimiak, A.9    Liu, J.10    Zhao, N.11    Rao, Z.12
  • 34
    • 0033135707 scopus 로고    scopus 로고
    • Crystal structure of an aminoglycoside 6'-N-acetyltransferase: Defining the GCN5-related N-acetyltransferase superfamily fold
    • DOI 10.1016/S0969-2126(99)80066-5
    • Wybenga-Groot, L. E., Draker, K., Wright, G. D. and Berghuis, A. M. (1999) Crystal structure of an aminoglycoside 6′-N-acetyltransferase: defining the GCN5-related N-acetyltransferase superfamily fold. Structure 7, 497-507 (Pubitemid 29230484)
    • (1999) Structure , vol.7 , Issue.5 , pp. 497-507
    • Wybenga-Groot, L.E.1    Draker, K.-A.2    Wright, G.D.3    Berghuis, A.M.4
  • 35
    • 0033579559 scopus 로고    scopus 로고
    • Crystal structure of the histone acetyltransferase Hpa2: A tetrameric member of the Gcn5-related N-acetyltransferase superfamily
    • DOI 10.1006/jmbi.1999.3338
    • Angus-Hill, M. L., Dutnall, R. N., Tafrov, S. T., Sternglanz, R. and Ramakrishnan, V. (1999) Crystal structure of the histone acetyltransferase Hpa2: a tetrameric member of the Gcn5-related N-acetyltransferase superfamily1. J. Mol. Biol. 294, 1311-1325 (Pubitemid 30008802)
    • (1999) Journal of Molecular Biology , vol.294 , Issue.5 , pp. 1311-1325
    • Angus-Hill, M.L.1    Dutnall, R.N.2    Tafrov, S.T.3    Sternglanz, R.4    Ramakrishnan, V.5
  • 36
    • 0035844169 scopus 로고    scopus 로고
    • The crystal structures of Apo and complexed Saccharomyces cerevisiae GNA1 shed light on the catalytic mechanism of an amino-sugar N-acetyltransferase
    • Peneff, C. (2001) The crystal structures of Apo and complexed Saccharomyces cerevisiae GNA1 shed light on the catalytic mechanism of an amino-sugar N-acetyltransferase. J. Biol. Chem. 276, 16328-16334
    • (2001) J. Biol. Chem. , vol.276 , pp. 16328-16334
    • Peneff, C.1
  • 39
    • 0019443447 scopus 로고
    • The anatomy and taxonomy of protein structure
    • Richardson, J. S. (1981) The anatomy and taxonomy of protein structure. Adv. Protein Chem. 34, 167-339
    • (1981) Adv. Protein Chem. , vol.34 , pp. 167-339
    • Richardson, J.S.1
  • 40
    • 0032898932 scopus 로고    scopus 로고
    • Saccharomyces cerevisiae GNA1, an essential gene encoding a novel acetyltransferase involved in UDP-N-acetylglucosamine synthesis
    • DOI 10.1074/jbc.274.1.424
    • Mio, T., Yamada-Okabe, T., Arisawa, M. and Yamada-Okabe, H. (1999) Saccharomyces cerevisiae GNA1, an essential gene encoding a novel acetyltransferase involved in UDP-N-acetylglucosamine synthesis. J. Biol. Chem. 274, 424-429 (Pubitemid 29035078)
    • (1999) Journal of Biological Chemistry , vol.274 , Issue.1 , pp. 424-429
    • Mio, M.1    Yamada-Okabe, T.2    Arisawa, M.3    Yamada-Okabe, H.4
  • 41
    • 0035917466 scopus 로고    scopus 로고
    • Crystal structure of the 14-3-3ζ:serotonin N-acetyltransferase complex: A role for scaffolding in enzyme regulation
    • DOI 10.1016/S0092-8674(01)00316-6
    • Obsil, T., Ghirlando, R., Klein, D. C., Ganguly, S. and Dyda, F. (2001) Crystal structure of the 14-3-3ζ:serotonin N-acetyltransferase complex. a role for scaffolding in enzyme regulation. Cell 105, 257-267 (Pubitemid 32429515)
    • (2001) Cell , vol.105 , Issue.2 , pp. 257-267
    • Obsil, T.1    Ghirlando, R.2    Klein, D.C.3    Ganguly, S.4    Dyda, F.5
  • 42
    • 0004262303 scopus 로고
    • Academic Press, New York
    • Dixon, M. and Webb, E. C. (1964) Enzymes. Academic Press, New York
    • (1964) Enzymes
    • Dixon, M.1    Webb, E.C.2
  • 43
    • 0034705440 scopus 로고    scopus 로고
    • Clarifying the catalytic roles of conserved residues in the amidase signature family
    • DOI 10.1074/jbc.M001607200
    • Patricelli, M. P. and Cravatt, B. F. (2000) Clarifying the catalytic roles of conserved residues in the amidase signature family. J. Biol. Chem. 275, 19177-19184 (Pubitemid 30422888)
    • (2000) Journal of Biological Chemistry , vol.275 , Issue.25 , pp. 19177-19184
    • Patricelli, M.P.1    Cravatt, B.F.2
  • 44
    • 0141733197 scopus 로고    scopus 로고
    • Evidence for distinct roles in catalysis for residues of the serine-serine-lysine catalytic triad of fatty acid amide hydrolase
    • DOI 10.1074/jbc.M303922200
    • McKinney, M. K. and Cravatt, B. F. (2003) Evidence for distinct roles in catalysis for residues of the serine-serine-lysine catalytic triad of fatty acid amide hydrolase. J. Biol. Chem. 278, 37393-37399 (Pubitemid 37175258)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.39 , pp. 37393-37399
    • McKinney, M.K.1    Cravatt, B.F.2
  • 45
    • 0036001159 scopus 로고    scopus 로고
    • a values of catalytic groups in enzyme active sites
    • DOI 10.1080/15216540211468
    • Harris, T. K. and Turner, G. J. (2002) Structural basis of perturbed pKa values of catalytic groups in enzyme active sites. IUBMB Life 53, 85-98 (Pubitemid 34553129)
    • (2002) IUBMB Life , vol.53 , Issue.2 , pp. 85-98
    • Harris, T.K.1    Turner, G.J.2
  • 46
    • 0026345864 scopus 로고
    • Structural and thermodynamic consequences of burying a charged residue within the hydrophobic core of T4 lysozyme
    • Dao-pin, S., Anderson, D. E., Baase, W. A., Dahlquist, F. W. and Matthews, B. W. (1991) Structural and thermodynamic consequences of burying a charged residue within the hydrophobic core of T4 lysozyme. Biochemistry 30, 11521-11529
    • (1991) Biochemistry , vol.30 , pp. 11521-11529
    • Dao-pin, S.1    Anderson, D.E.2    Baase, W.A.3    Dahlquist, F.W.4    Matthews, B.W.5
  • 47
    • 0026042631 scopus 로고
    • Reengineering the catalytic lysine of aspartate aminotransferase by chemical elaboration of a genetically introduced cysteine
    • Planas, A. and Kirsch, J. F. (1991) Reengineering the catalytic lysine of aspartate aminotransferase by chemical elaboration of a genetically introduced cysteine. Biochemistry 30, 8268-8276
    • (1991) Biochemistry , vol.30 , pp. 8268-8276
    • Planas, A.1    Kirsch, J.F.2
  • 49
    • 17644384428 scopus 로고    scopus 로고
    • Role of a conserved glutamate residue in the Escherichia coli SecA ATPase mechanism
    • DOI 10.1074/jbc.M414224200
    • Zito, C. R., Antony, E., Hunt, J. F., Oliver, D. B. and Hingorani, M. M. (2005) Role of a conserved glutamate residue in the Escherichia coli SecA ATPase mechanism. J. Biol. Chem. 280, 14611-14619 (Pubitemid 40562806)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.15 , pp. 14611-14619
    • Zito, C.R.1    Antony, E.2    Hunt, J.F.3    Oliver, D.B.4    Hingorani, M.M.5
  • 50
    • 0028854034 scopus 로고
    • Molecular recognition of receptor sites using a genetic algorithm with a description of desolvation
    • Jones, G., Willett, P. and Glen, R. C. (1995) Molecular recognition of receptor sites using a genetic algorithm with a description of desolvation. J. Mol. Biol. 245, 43-53
    • (1995) J. Mol. Biol. , vol.245 , pp. 43-53
    • Jones, G.1    Willett, P.2    Glen, R.C.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.