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Volumn 65, Issue 1, 2006, Pages 220-230

Crystal structures of the PLP- and PMP-bound forms of BtrR, a dual functional aminotransferase involved in butirosin biosynthesis

Author keywords

Aminoglycoside antibiotics; Aminotransferase; Butirosin; Secondary metabolite aminotransferases (SMAT); X ray crystallography

Indexed keywords

2 DEOXYINOSAMINE; 2 DEOXYSCYLLOINOSOSE; 2 DEOXYSTREPTAMINE; AMINODIDEOXYSCYLLOINOSOSE; AMINOGLYCOSIDE ANTIBIOTIC AGENT; AMINOTRANSFERASE; ASPARTIC ACID; BACTERIAL ENZYME; BUTIROSIN; GLYCOSIDE; HOMODIMER; PROTEIN BTRR; PYRIDOXAL 5 PHOSPHATE; PYRIDOXAMINE PHOSPHATE; TRYPTOPHAN; TYROSINE; UNCLASSIFIED DRUG;

EID: 33748255080     PISSN: 08873585     EISSN: 10970134     Source Type: Journal    
DOI: 10.1002/prot.21076     Document Type: Article
Times cited : (16)

References (33)
  • 1
    • 0042337397 scopus 로고    scopus 로고
    • Molecular recognition of aminoglycoside antibiotics by ribosomal RNA and resistance enzymes: An analysis of x-ray crystal structures
    • Vicens Q, Westhof E. Molecular recognition of aminoglycoside antibiotics by ribosomal RNA and resistance enzymes: an analysis of x-ray crystal structures. Biopolymers 2003;70:42-57.
    • (2003) Biopolymers , vol.70 , pp. 42-57
    • Vicens, Q.1    Westhof, E.2
  • 3
    • 0035908235 scopus 로고    scopus 로고
    • Convenient synthesis of 2-deoxy-scyllo-inosose and 2-deoxyscyllo- inosamine: Two key intermediates on the biosynthetic pathway to aminoglycoside antibiotics
    • Yu J. Convenient synthesis of 2-deoxy-scyllo-inosose and 2-deoxyscyllo-inosamine: two key intermediates on the biosynthetic pathway to aminoglycoside antibiotics. Tetrahedron Lett 2001;42:4219-4221.
    • (2001) Tetrahedron Lett , vol.42 , pp. 4219-4221
    • Yu, J.1
  • 4
    • 0036671912 scopus 로고    scopus 로고
    • Identification of L-glutamine: 2-Deoxy-scyllo-inosose aminotransferase required for the biosynthesis of butirosin in Bacillus circulans
    • Tamegai H, et al. Identification of L-glutamine: 2-deoxy-scyllo-inosose aminotransferase required for the biosynthesis of butirosin in Bacillus circulans. J Antibiot (Tokyo) 2002;55:707-714.
    • (2002) J Antibiot (Tokyo) , vol.55 , pp. 707-714
    • Tamegai, H.1
  • 5
    • 0036436618 scopus 로고    scopus 로고
    • Biosynthesis of aminoglycoside antibiotics: Cloning, expression and characterisation of an aminotransferase involved in the pathway to 2-deoxystreptamine
    • Huang F, Li Y, Yu J, Spencer JB. Biosynthesis of aminoglycoside antibiotics: cloning, expression and characterisation of an aminotransferase involved in the pathway to 2-deoxystreptamine. Chem Commun (Camb) 2002;2860-2861.
    • (2002) Chem Commun (Camb) , pp. 2860-2861
    • Huang, F.1    Li, Y.2    Yu, J.3    Spencer, J.B.4
  • 6
    • 17744378979 scopus 로고    scopus 로고
    • Stereochemical recognition of doubly functional aminotransferase in 2-deoxystreptamine biosynthesis
    • Yokoyama K, et al. Stereochemical recognition of doubly functional aminotransferase in 2-deoxystreptamine biosynthesis. J Am Chem Soc 2005;127:5869-5874.
    • (2005) J Am Chem Soc , vol.127 , pp. 5869-5874
    • Yokoyama, K.1
  • 8
    • 0035967880 scopus 로고    scopus 로고
    • FUGUE: Sequence-structure homology recognition using environment-specific substitution tables and structure-dependent gap penalties
    • Shi J, Blundell TL, Mizuguchi K. FUGUE: sequence-structure homology recognition using environment-specific substitution tables and structure-dependent gap penalties. J Mol Biol 2001;310:243-257.
    • (2001) J Mol Biol , vol.310 , pp. 243-257
    • Shi, J.1    Blundell, T.L.2    Mizuguchi, K.3
  • 9
    • 0025283867 scopus 로고
    • Use of T7 RNA polymerase to direct expression of cloned genes
    • Studier WF, Dunn JJ, Dubendorff JW. Use of T7 RNA polymerase to direct expression of cloned genes. Methods Enzymol 1990;185:60-89.
    • (1990) Methods Enzymol , vol.185 , pp. 60-89
    • Studier, W.F.1    Dunn, J.J.2    Dubendorff, J.W.3
  • 10
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Otwinowski Z, Minor W. Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol 1997;276:307-326.
    • (1997) Methods Enzymol , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 11
    • 0028103275 scopus 로고
    • The CCP4 suite: Programs for protein crystallography
    • Project CC. The CCP4 suite: programs for protein crystallography. Acta Crystallogr D Biol Crystallogr 1994;50:760-763.
    • (1994) Acta Crystallogr D Biol Crystallogr , vol.50 , pp. 760-763
    • Project, C.C.1
  • 12
    • 84920325457 scopus 로고
    • AMoRe: An automated package for molecular replacement
    • Navaza J. AMoRe: an automated package for molecular replacement. Acta Crystallogr D Biol Crystallogr 1994;50:157-163.
    • (1994) Acta Crystallogr D Biol Crystallogr , vol.50 , pp. 157-163
    • Navaza, J.1
  • 14
    • 0032790081 scopus 로고    scopus 로고
    • XtalView/Xfit - A versatile program for manipulating atomic coordinates and electron density
    • McRee DE. XtalView/Xfit-a versatile program for manipulating atomic coordinates and electron density. J Struct Biol 1999;125:156-165.
    • (1999) J Struct Biol , vol.125 , pp. 156-165
    • McRee, D.E.1
  • 16
    • 0030814692 scopus 로고    scopus 로고
    • Identification of stsC, the gene encoding the L-glutamine:scyllo-mosose aminotransferase from streptomycin-producing Streptomycetes
    • Ahlert J, Distler J, Mansouri K, Piepersberg W. Identification of stsC, the gene encoding the L-glutamine:scyllo-mosose aminotransferase from streptomycin-producing Streptomycetes. Arch Microbiol 1997;168:102-113.
    • (1997) Arch Microbiol , vol.168 , pp. 102-113
    • Ahlert, J.1    Distler, J.2    Mansouri, K.3    Piepersberg, W.4
  • 17
    • 0000243829 scopus 로고
    • PRO-CHECK: A program to check the stereochemical quality of protein structures
    • Laskowski RA, MacArthur MW, Moss DS, Thornton JM. PRO-CHECK: a program to check the stereochemical quality of protein structures. J Appl Cryst 1993;26:283-291.
    • (1993) J Appl Cryst , vol.26 , pp. 283-291
    • Laskowski, R.A.1    MacArthur, M.W.2    Moss, D.S.3    Thornton, J.M.4
  • 18
    • 0033520088 scopus 로고    scopus 로고
    • Crystal structure of 3-amino-5-hydroxybenzoic acid (AHBA) synthase
    • Eads JC, Beeby M, Scapin G, Yu TW, Floss HG. Crystal structure of 3-amino-5-hydroxybenzoic acid (AHBA) synthase. Biochemistry 1999;38:9840-9849.
    • (1999) Biochemistry , vol.38 , pp. 9840-9849
    • Eads, J.C.1    Beeby, M.2    Scapin, G.3    Yu, T.W.4    Floss, H.G.5
  • 19
    • 0031800056 scopus 로고    scopus 로고
    • Crystal structure of Saccharomyces cerevisiae cytosolic aspartate aminotransferase
    • Jeffery CJ, Barry T, Doonan S, Petsko GA, Ringe D. Crystal structure of Saccharomyces cerevisiae cytosolic aspartate aminotransferase. Protein Sci 1998;7:1380-1387.
    • (1998) Protein Sci , vol.7 , pp. 1380-1387
    • Jeffery, C.J.1    Barry, T.2    Doonan, S.3    Petsko, G.A.4    Ringe, D.5
  • 20
    • 0242538842 scopus 로고    scopus 로고
    • Crystal structure of diaminopelargonic acid synthase: Evolutionary relationships between pyridoxal-5′-phosphate-dependent enzymes
    • Rack H, Sandmark J, Gibson K, Schneider G, Lindqvist Y. Crystal structure of diaminopelargonic acid synthase: evolutionary relationships between pyridoxal-5′-phosphate-dependent enzymes. J Mol Biol 1999;291:857-876.
    • (1999) J Mol Biol , vol.291 , pp. 857-876
    • Rack, H.1    Sandmark, J.2    Gibson, K.3    Schneider, G.4    Lindqvist, Y.5
  • 23
    • 0030845064 scopus 로고    scopus 로고
    • Refinement and comparisons of the crystal structures of pig cytosolic aspartate aminotransferase and its complex with 2-methylaspartate
    • Rhee S, Silva MM, Hyde CC, Rogers PH, Metzler CM, Metzler DE, Arnone A. Refinement and comparisons of the crystal structures of pig cytosolic aspartate aminotransferase and its complex with 2-methylaspartate. J Biol Chem 1997;272:17293-17302.
    • (1997) J Biol Chem , vol.272 , pp. 17293-17302
    • Rhee, S.1    Silva, M.M.2    Hyde, C.C.3    Rogers, P.H.4    Metzler, C.M.5    Metzler, D.E.6    Arnone, A.7
  • 24
    • 0027536099 scopus 로고
    • A hydrogen-bonding network modulating enzyme function: Asparagine-194 and tyrosine-225 of Escherichia coli aspartate aminotransferase
    • Yano T, Mizuno T, Kagamiyama H. A hydrogen-bonding network modulating enzyme function: asparagine-194 and tyrosine-225 of Escherichia coli aspartate aminotransferase. Biochemistry 1993;32:1810-1815.
    • (1993) Biochemistry , vol.32 , pp. 1810-1815
    • Yano, T.1    Mizuno, T.2    Kagamiyama, H.3
  • 25
    • 0025317502 scopus 로고
    • Definition of general topological equivalence in protein structures. A procedure involving comparison of properties and relationships through simulated annealing and dynamic programming
    • Sali A, Blundell TL. Definition of general topological equivalence in protein structures. A procedure involving comparison of properties and relationships through simulated annealing and dynamic programming. J Mol Biol 1990;212:403-428.
    • (1990) J Mol Biol , vol.212 , pp. 403-428
    • Sali, A.1    Blundell, T.L.2
  • 26
    • 0041989751 scopus 로고    scopus 로고
    • CASTp: Computed Atlas of Surface Topography of proteins
    • Binkowski TA, Naghibzadeh S, Liang J. CASTp: Computed Atlas of Surface Topography of proteins. Nucleic Acids Res 2003;31:3352-3355.
    • (2003) Nucleic Acids Res , vol.31 , pp. 3352-3355
    • Binkowski, T.A.1    Naghibzadeh, S.2    Liang, J.3
  • 28
    • 16644397843 scopus 로고    scopus 로고
    • Developments in the CCP4 molecular-graphics project
    • Potterton L, et al. Developments in the CCP4 molecular-graphics project. Acta Crystallogr D Biol Crystallogr 2004;60:2288-2294.
    • (2004) Acta Crystallogr D Biol Crystallogr , vol.60 , pp. 2288-2294
    • Potterton, L.1
  • 29
    • 0026504874 scopus 로고
    • Mechanism of racemization of amino acids by aspartate aminotransferase
    • Kochhar S, Christen P. Mechanism of racemization of amino acids by aspartate aminotransferase. Eur J Biochem 1992;203:563-569.
    • (1992) Eur J Biochem , vol.203 , pp. 563-569
    • Christen P, K.S.1
  • 30
    • 0036850945 scopus 로고    scopus 로고
    • Structural studies of Salmonella typhimurium ArnB (PmrH) aminotransferase: A 4-amino-4-deoxy-L-arabinose lipopolysaccharide-modifying enzyme
    • Noland BW, et al. Structural studies of Salmonella typhimurium ArnB (PmrH) aminotransferase: a 4-amino-4-deoxy-L-arabinose lipopolysaccharide- modifying enzyme. Structure (Camb) 2002;10:1569-1580.
    • (2002) Structure (Camb) , vol.10 , pp. 1569-1580
    • Noland, B.W.1
  • 31
    • 0042377122 scopus 로고    scopus 로고
    • Structure, catalytic activity and evolutionary relationships of 1-aminocyclopropane-1-carboxylate synthase, the key enzyme of ethylene synthesis in higher plants
    • Jakubowicz M. Structure, catalytic activity and evolutionary relationships of 1-aminocyclopropane-1-carboxylate synthase, the key enzyme of ethylene synthesis in higher plants. Acta Biochim Pol 2002;49:757-774.
    • (2002) Acta Biochim Pol , vol.49 , pp. 757-774
    • Jakubowicz, M.1
  • 32
    • 3943113663 scopus 로고    scopus 로고
    • Pyridoxal phosphate enzymes: Mechanistic, structural, and evolutionary considerations
    • Eliot AC, Kirsch JF. Pyridoxal phosphate enzymes: mechanistic, structural, and evolutionary considerations. Annu Rev Biochem 2004;73:383-415.
    • (2004) Annu Rev Biochem , vol.73 , pp. 383-415
    • Eliot, A.C.1    Kirsch, J.F.2


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