메뉴 건너뛰기




Volumn 23, Issue 9, 2013, Pages 1075-1083

The structure of the Mycobacterium smegmatis trehalose synthase reveals an unusual active site configuration and acarbose-binding mode

Author keywords

Drug design; Enzyme inhibition; GH13 glycoside hydrolase; Trehalose synthase; Tuberculosis

Indexed keywords

ACARBOSE; BACTERIAL ENZYME; SYNTHETASE; TREHALOSE SYNTHASE; UNCLASSIFIED DRUG;

EID: 84880926719     PISSN: 09596658     EISSN: 14602423     Source Type: Journal    
DOI: 10.1093/glycob/cwt044     Document Type: Article
Times cited : (44)

References (59)
  • 4
    • 0030200404 scopus 로고    scopus 로고
    • Drug sensitivity and environmental adaptation of mycobacterial cell wall components
    • Barry CE, III, Mdluli K. 1996. Drug sensitivity and environmental adaptation of mycobacterial cell wall components. Trends Microbiol. 4: 275-281.
    • (1996) Trends Microbiol , vol.4 , pp. 275-281
    • Barry III, C.E.1    Mdluli, K.2
  • 5
    • 4744368323 scopus 로고    scopus 로고
    • Carbohydrate-binding modules: Fine-tuning polysaccharide recognition
    • Boraston AB, Bolam DN, Gilbert HJ, Davies GJ. 2004. Carbohydrate-binding modules: Fine-tuning polysaccharide recognition. Biochem J. 382: 769-781.
    • (2004) Biochem J , vol.382 , pp. 769-781
    • Boraston, A.B.1    Bolam, D.N.2    Gilbert, H.J.3    Davies, G.J.4
  • 6
    • 34547117839 scopus 로고
    • Mechanism of enzyme action
    • Boyer PD. 1960. Mechanism of enzyme action. Annu Rev Biochem. 29: 15-44.
    • (1960) Annu Rev Biochem , vol.29 , pp. 15-44
    • Boyer, P.D.1
  • 7
    • 0029111443 scopus 로고
    • The structure of human pancreatic alpha-amylase at 1.8 A resolution and comparisons with related enzymes
    • Brayer GD, Luo Y, Withers SG. 1995. The structure of human pancreatic alpha-amylase at 1.8 A resolution and comparisons with related enzymes. Protein Sci. 4: 1730-1742.
    • (1995) Protein Sci , vol.4 , pp. 1730-1742
    • Brayer, G.D.1    Luo, Y.2    Withers, S.G.3
  • 10
    • 0348053809 scopus 로고
    • Preservation of membranes in anhydrobiotic organisms: The role of trehalose
    • Crowe JH, Crowe LM, Chapman D. 1984. Preservation of membranes in anhydrobiotic organisms: The role of trehalose. Science. 223: 701-703.
    • (1984) Science , vol.223 , pp. 701-703
    • Crowe, J.H.1    Crowe, L.M.2    Chapman, D.3
  • 11
    • 0032452982 scopus 로고    scopus 로고
    • The envelope layers of mycobacteria with reference to their pathogenicity
    • Daffe M, Draper P. 1998. The envelope layers of mycobacteria with reference to their pathogenicity. Adv Microb Physiol. 39: 131-203.
    • (1998) Adv Microb Physiol , vol.39 , pp. 131-203
    • Daffe, M.1    Draper, P.2
  • 13
    • 40449114454 scopus 로고    scopus 로고
    • Metals in proteins: Correlation between the metal-ion type, coordination number and the amino-acid residues involved in the coordination
    • Dokmanic I, Sikic M, Tomic S. 2008. Metals in proteins: Correlation between the metal-ion type, coordination number and the amino-acid residues involved in the coordination. Acta Crystallogr D Biol Crystallogr. 64: 257-263.
    • (2008) Acta Crystallogr D Biol Crystallogr , vol.64 , pp. 257-263
    • Dokmanic, I.1    Sikic, M.2    Tomic, S.3
  • 14
    • 0016305880 scopus 로고
    • The metabolism of alpha, alpha-trehalose
    • Elbein AD. 1974. The metabolism of alpha, alpha-trehalose. Adv Carbohydr Chem Biochem. 30: 227-256.
    • (1974) Adv Carbohydr Chem Biochem , vol.30 , pp. 227-256
    • Elbein, A.D.1
  • 15
    • 77951245174 scopus 로고    scopus 로고
    • Last step in the conversion of trehalose to glycogen: A mycobacterial enzyme that transfers maltose from maltose 1-phosphate to glycogen
    • Elbein AD, Pastuszak I, Tackett AJ, Wilson T, Pan YT. 2010. Last step in the conversion of trehalose to glycogen: A mycobacterial enzyme that transfers maltose from maltose 1-phosphate to glycogen. J Biol Chem. 285: 9803-9812.
    • (2010) J Biol Chem , vol.285 , pp. 9803-9812
    • Elbein, A.D.1    Pastuszak, I.2    Tackett, A.J.3    Wilson, T.4    Pan, Y.T.5
  • 16
    • 1442323775 scopus 로고    scopus 로고
    • Ligand-mediated dimerization of a carbohydrate-binding molecule reveals a novel mechanism for protein-carbohydrate recognition
    • Flint J, Nurizzo D, Harding SE, Longman E, Davies GJ, Gilbert HJ, Bolam DN. 2004. Ligand-mediated dimerization of a carbohydrate-binding molecule reveals a novel mechanism for protein-carbohydrate recognition. J Mol Biol. 337: 417-426.
    • (2004) J Mol Biol , vol.337 , pp. 417-426
    • Flint, J.1    Nurizzo, D.2    Harding, S.E.3    Longman, E.4    Davies, G.J.5    Gilbert, H.J.6    Bolam, D.N.7
  • 17
    • 0023644474 scopus 로고
    • The three-dimensional structure of acarbose bound to glycogen phosphorylase
    • Goldsmith EJ, Fletterick RJ, Withers SG. 1987. The three-dimensional structure of acarbose bound to glycogen phosphorylase. J Biol Chem. 262: 1449-1455.
    • (1987) J Biol Chem , vol.262 , pp. 1449-1455
    • Goldsmith, E.J.1    Fletterick, R.J.2    Withers, S.G.3
  • 18
    • 0033179802 scopus 로고    scopus 로고
    • The geometry of metal-ligand interactions relevant to proteins
    • Harding MM. 1999. The geometry of metal-ligand interactions relevant to proteins. Acta Crystallogr D Biol Crystallogr. 55: 1432-1443.
    • (1999) Acta Crystallogr D Biol Crystallogr , vol.55 , pp. 1432-1443
    • Harding, M.M.1
  • 19
    • 0033937430 scopus 로고    scopus 로고
    • The geometry of metal-ligand interactions relevant to proteins. II. Angles at the metal atom, additional weak metal-donor interactions
    • Harding MM. 2000. The geometry of metal-ligand interactions relevant to proteins. II. Angles at the metal atom, additional weak metal-donor interactions. Acta Crystallogr D Biol Crystallogr. 56: 857-867.
    • (2000) Acta Crystallogr D Biol Crystallogr , vol.56 , pp. 857-867
    • Harding, M.M.1
  • 20
    • 0035094475 scopus 로고    scopus 로고
    • Geometry of metal-ligand interactions in proteins
    • Harding MM. 2001. Geometry of metal-ligand interactions in proteins. Acta Crystallogr D Biol Crystallogr. 57: 401-411.
    • (2001) Acta Crystallogr D Biol Crystallogr , vol.57 , pp. 401-411
    • Harding, M.M.1
  • 21
    • 4644355809 scopus 로고    scopus 로고
    • The architecture of metal coordination groups in proteins
    • Harding MM. 2004. The architecture of metal coordination groups in proteins. Acta Crystallogr D Biol Crystallogr. 60: 849-859.
    • (2004) Acta Crystallogr D Biol Crystallogr , vol.60 , pp. 849-859
    • Harding, M.M.1
  • 22
    • 33744502092 scopus 로고    scopus 로고
    • Small revisions to predicted distances around metal sites in proteins
    • Harding MM. 2006. Small revisions to predicted distances around metal sites in proteins. Acta Crystallogr D Biol Crystallogr. 62: 678-682.
    • (2006) Acta Crystallogr D Biol Crystallogr , vol.62 , pp. 678-682
    • Harding, M.M.1
  • 23
    • 0037293103 scopus 로고    scopus 로고
    • Relation between domain evolution, specificity, and taxonomy of the alpha-amylase family members containing a C-terminal starch-binding domain
    • Janecek S, Svensson B, MacGregor EA. 2003. Relation between domain evolution, specificity, and taxonomy of the alpha-amylase family members containing a C-terminal starch-binding domain. Eur J Biochem. 270: 635-645.
    • (2003) Eur J Biochem , vol.270 , pp. 635-645
    • Janecek, S.1    Svensson, B.2    MacGregor, E.A.3
  • 24
    • 0026541540 scopus 로고
    • Molecular cloning and physical mapping of the ots BA genes, which encode the osmoregulatory trehalose pathway of Escherichia coli: Evidence that transcription is activated by kat F (AppR)
    • Kaasen I, Falkenberg P, Styrvold OB, Strom AR. 1992. Molecular cloning and physical mapping of the ots BA genes, which encode the osmoregulatory trehalose pathway of Escherichia coli: Evidence that transcription is activated by kat F (AppR). J Bacteriol 174: 889-898.
    • (1992) J Bacteriol , vol.174 , pp. 889-898
    • Kaasen, I.1    Falkenberg, P.2    Styrvold, O.B.3    Strom, A.R.4
  • 26
    • 79954442657 scopus 로고    scopus 로고
    • The significance of GlgE as a new target for tuberculosis
    • Kalscheuer R, Jacobs WR, Jr. 2010. The significance of GlgE as a new target for tuberculosis. Drug News Perspect. 23: 619-624.
    • (2010) Drug News Perspect , vol.23 , pp. 619-624
    • Kalscheuer, R.1    Jacobs Jr., W.R.2
  • 28
    • 84861425552 scopus 로고    scopus 로고
    • Linking crystallographic model and data quality
    • Karplus PA, Diederichs K. 2012. Linking crystallographic model and data quality. Science. 336: 1030-1033.
    • (2012) Science , vol.336 , pp. 1030-1033
    • Karplus, P.A.1    Diederichs, K.2
  • 29
    • 84979146389 scopus 로고
    • Stereochemistry and the mechanism of enzymatic reactions
    • Koshland DE. 1953. Stereochemistry and the mechanism of enzymatic reactions. Biol. Rev. 28: 416-436.
    • (1953) Biol. Rev , vol.28 , pp. 416-436
    • Koshland, D.E.1
  • 30
    • 72449167058 scopus 로고    scopus 로고
    • Crystal contacts as nature's docking solutions
    • Krissinel E. 2010. Crystal contacts as nature's docking solutions. J Comput Chem. 31: 133-143.
    • (2010) J Comput Chem , vol.31 , pp. 133-143
    • Krissinel, E.1
  • 31
    • 34548232365 scopus 로고    scopus 로고
    • Inference of macromolecular assemblies from crystalline state
    • Krissinel E, Henrick K. 2007. Inference of macromolecular assemblies from crystalline state. J Mol Biol. 372: 774-797.
    • (2007) J Mol Biol , vol.372 , pp. 774-797
    • Krissinel, E.1    Henrick, K.2
  • 32
    • 0032976301 scopus 로고    scopus 로고
    • The concept of the alpha-amylase family: Structural similarity and common catalytic mechanism
    • Kuriki T, Imanaka T. 1999. The concept of the alpha-amylase family: Structural similarity and common catalytic mechanism. J Biosci Bioeng. 87: 557-565.
    • (1999) J Biosci Bioeng , vol.87 , pp. 557-565
    • Kuriki, T.1    Imanaka, T.2
  • 33
    • 80054911951 scopus 로고    scopus 로고
    • Lig Plot+: Multiple ligand-protein interaction diagrams for drug discovery
    • Laskowski RA, Swindells MB. 2011. Lig Plot+: Multiple ligand-protein interaction diagrams for drug discovery. J Chem Inf Model. 51: 2778-2786.
    • (2011) J Chem Inf Model , vol.51 , pp. 2778-2786
    • Laskowski, R.A.1    Swindells, M.B.2
  • 34
    • 33751330163 scopus 로고    scopus 로고
    • Quaternary structure and enzymatic properties of cyclomaltodextrinase from alkalophilic Bacillus sp. I-5
    • Lee H-s, Kim J-s, Shim K-h, Kim J-w, Park C-s, Park K-h. 2005. Quaternary structure and enzymatic properties of cyclomaltodextrinase from alkalophilic Bacillus sp. I-5. Biologia Bratislava. 60: 73-77.
    • (2005) Biologia Bratislava , vol.60 , pp. 73-77
    • Lee, H.-S.1    Kim, J.-S.2    Shim, K.-H.3    Kim, J.-W.4    Park, C.-S.5    Park, K.-H.6
  • 35
    • 0015975824 scopus 로고
    • The allosteric activation of mammalian alpha-amylase by chloride
    • Levitzki A, Steer ML. 1974. The allosteric activation of mammalian alpha-amylase by chloride. Eur J Biochem. 41: 171-180.
    • (1974) Eur J Biochem , vol.41 , pp. 171-180
    • Levitzki, A.1    Steer, M.L.2
  • 36
    • 0017130015 scopus 로고
    • Identity and properties of the chloride effector binding site in hog pancreatic alpha-amylase
    • Lifshitz R, Levitzki A. 1976. Identity and properties of the chloride effector binding site in hog pancreatic alpha-amylase. Biochemistry (Mosc). 15: 1987-1993.
    • (1976) Biochemistry (Mosc) , vol.15 , pp. 1987-1993
    • Lifshitz, R.1    Levitzki, A.2
  • 39
    • 0030573162 scopus 로고    scopus 로고
    • Cloning and sequencing of a cluster of genes encoding novel enzymes of trehalose biosynthesis from thermophilic archaebacterium Sulfolobus acidocaldarius
    • Maruta K, Mitsuzumi H, Nakada T, Kubota M, Chaen H, Fukuda S, Sugimoto T, Kurimoto M. 1996c. Cloning and sequencing of a cluster of genes encoding novel enzymes of trehalose biosynthesis from thermophilic archaebacterium Sulfolobus acidocaldarius. Biochim Biophys Acta. 1291: 177-181.
    • (1996) Biochim Biophys Acta , vol.1291 , pp. 177-181
    • Maruta, K.1    Mitsuzumi, H.2    Nakada, T.3    Kubota, M.4    Chaen, H.5    Fukuda, S.6    Sugimoto, T.7    Kurimoto, M.8
  • 41
    • 33846426122 scopus 로고    scopus 로고
    • Solving structures of protein complexes by molecular replacement with Phaser
    • McCoy AJ. 2007. Solving structures of protein complexes by molecular replacement with Phaser. Acta Crystallogr D Biol Crystallogr. 63: 32-41.
    • (2007) Acta Crystallogr D Biol Crystallogr , vol.63 , pp. 32-41
    • McCoy, A.J.1
  • 42
    • 84876459348 scopus 로고    scopus 로고
    • Flux through trehalose synthase flows from trehalose to the alpha anomer of maltose in mycobacteria
    • Miah F, Koliwer-Brandl H, Rejzek M, Field RA, Kalscheuer R, Bornemann S. 2013. Flux through trehalose synthase flows from trehalose to the alpha anomer of maltose in mycobacteria. Chem Biol. 20: 487-493.
    • (2013) Chem Biol , vol.20 , pp. 487-493
    • Miah, F.1    Koliwer-Brandl, H.2    Rejzek, M.3    Field, R.A.4    Kalscheuer, R.5    Bornemann, S.6
  • 43
  • 45
    • 0036866921 scopus 로고    scopus 로고
    • Oligo-1, 6-glucosidase and neopullulanase enzyme subfamilies from the alpha-amylase family defined by the fifth conserved sequence region
    • Oslancova A, Janecek S. 2002. Oligo-1, 6-glucosidase and neopullulanase enzyme subfamilies from the alpha-amylase family defined by the fifth conserved sequence region. Cell Mol Life Sci. 59: 1945-1959.
    • (2002) Cell Mol Life Sci , vol.59 , pp. 1945-1959
    • Oslancova, A.1    Janecek, S.2
  • 48
    • 0027296794 scopus 로고
    • Structure and molecular model refinement of pig pancreatic alpha-amylase at 2.1 A resolution
    • Qian M, Haser R, Payan F. 1993. Structure and molecular model refinement of pig pancreatic alpha-amylase at 2.1 A resolution. J Mol Biol. 231: 785-799.
    • (1993) J Mol Biol , vol.231 , pp. 785-799
    • Qian, M.1    Haser, R.2    Payan, F.3
  • 49
    • 34948875934 scopus 로고    scopus 로고
    • Trehalulose synthase native and carbohydrate complexed structures provide insights into sucrose isomerization
    • Ravaud S, Robert X, Watzlawick H, Haser R, Mattes R, Aghajari N. 2007. Trehalulose synthase native and carbohydrate complexed structures provide insights into sucrose isomerization. J Biol Chem. 282: 28126-28136.
    • (2007) J Biol Chem , vol.282 , pp. 28126-28136
    • Ravaud, S.1    Robert, X.2    Watzlawick, H.3    Haser, R.4    Mattes, R.5    Aghajari, N.6
  • 50
    • 33845665889 scopus 로고    scopus 로고
    • Dividing the large glycoside hydrolase family 13 into subfamilies: Towards improved functional annotations of alpha-amylase-related proteins
    • Stam MR, Danchin EG, Rancurel C, Coutinho PM, Henrissat B. 2006. Dividing the large glycoside hydrolase family 13 into subfamilies: Towards improved functional annotations of alpha-amylase-related proteins. Protein Eng Des Sel. 19: 555-562.
    • (2006) Protein Eng des Sel , vol.19 , pp. 555-562
    • Stam, M.R.1    Danchin, E.G.2    Rancurel, C.3    Coutinho, P.M.4    Henrissat, B.5
  • 51
    • 43749083257 scopus 로고    scopus 로고
    • CHAINSAW: A program for mutating pdb files used as templates in molecular replacement
    • Stein N. 2008. CHAINSAW: A program for mutating pdb files used as templates in molecular replacement. J Appl Cryst. 41: 641-643.
    • (2008) J Appl Cryst , vol.41 , pp. 641-643
    • Stein, N.1
  • 52
    • 0028429952 scopus 로고
    • Protein engineering in the alpha-amylase family: Catalytic mechanism, substrate specificity, and stability
    • Svensson B. 1994. Protein engineering in the alpha-amylase family: Catalytic mechanism, substrate specificity, and stability. Plant Mol Biol. 25: 141-157.
    • (1994) Plant Mol Biol , vol.25 , pp. 141-157
    • Svensson, B.1
  • 53
    • 0017259001 scopus 로고
    • Isolation, characterization, and function of 6-mycolyl-6′- acetyltrehalose in the H37Ra strain of Myocobacterium tuberculosis
    • Takayama K, Armstrong EL. 1976. Isolation, characterization, and function of 6-mycolyl-6′-acetyltrehalose in the H37Ra strain of Myocobacterium tuberculosis. Biochemistry (Mosc). 15: 441-447.
    • (1976) Biochemistry (Mosc) , vol.15 , pp. 441-447
    • Takayama, K.1    Armstrong, E.L.2
  • 55
    • 0025868757 scopus 로고
    • Thermodynamics of hydrolysis of disaccharides. Lactulose, alpha-D-melibiose, palatinose, D-trehalose, D-turanose and 3-o-beta-D- galactopyranosyl-D-arabinose
    • Tewari YB, Goldberg RN. 1991. Thermodynamics of hydrolysis of disaccharides. Lactulose, alpha-D-melibiose, palatinose, D-trehalose, D-turanose and 3-o-beta-D-galactopyranosyl-D-arabinose. Biophys Chem. 40: 59-67.
    • (1991) Biophys Chem , vol.40 , pp. 59-67
    • Tewari, Y.B.1    Goldberg, R.N.2
  • 56
    • 0012328038 scopus 로고    scopus 로고
    • Studies on the C-terminal region of barley α-amylase 1 with emphasis on raw starch-binding
    • Tibbot BK, Wong DWS, Robertson GH. 2002. Studies on the C-terminal region of barley α-amylase 1 with emphasis on raw starch-binding. Biologia Bratislava. 57: 229-238.
    • (2002) Biologia Bratislava , vol.57 , pp. 229-238
    • Tibbot, B.K.1    Wong, D.W.S.2    Robertson, G.H.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.