메뉴 건너뛰기




Volumn 276, Issue 3, 1998, Pages 591-602

Crystal structure of the IIB subunit of a fructose permease (IIB(Lev)) from Bacillus subtilis

Author keywords

Phosphotransferase system; PTS; Sugar transport; X ray structure

Indexed keywords

BACTERIAL ENZYME; FRUCTOSE PERMEASE; PERMEASE; PHOSPHOENOLPYRUVATE; UNCLASSIFIED DRUG;

EID: 0032570740     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.1997.1544     Document Type: Article
Times cited : (39)

References (51)
  • 1
    • 0031042397 scopus 로고    scopus 로고
    • The NMR side-chain assignments and solution structure of enzyme IIBcellobiose of the phosphoenolpyruvate-dependent phosphotransferase system of E. coli
    • Ab E., Schuurmann-Wolters G., Reizer J., Saier M. H., Dijkstra K., Scheek R. M., Robillard G. T. The NMR side-chain assignments and solution structure of enzyme IIBcellobiose of the phosphoenolpyruvate-dependent phosphotransferase system of E. coli. Protein Sci. 6:1997;304-314.
    • (1997) Protein Sci. , vol.6 , pp. 304-314
    • Ab, E.1    Schuurmann-Wolters, G.2    Reizer, J.3    Saier, M.H.4    Dijkstra, K.5    Scheek, R.M.6    Robillard, G.T.7
  • 2
    • 0027163002 scopus 로고
    • The involvement of the arginine-17 residue in the active site of the histidine-containing protein, HPr, of the phosphoenolpyruvate-sugar phosphotransferase system of Escherichia coli
    • Anderson J. W., Pullen K., Georges F., Klevit R. E., Waygood E. B. The involvement of the arginine-17 residue in the active site of the histidine-containing protein, HPr, of the phosphoenolpyruvate-sugar phosphotransferase system of Escherichia coli. J. Biol. Chem. 268:1993;12325-12333.
    • (1993) J. Biol. Chem. , vol.268 , pp. 12325-12333
    • Anderson, J.W.1    Pullen, K.2    Georges, F.3    Klevit, R.E.4    Waygood, E.B.5
  • 5
    • 0016327034 scopus 로고
    • Structure of yeast phosphoglycerate mutase
    • Campbell J. W., Watson H. C., Hodgson G. I. Structure of yeast phosphoglycerate mutase. Nature. 250:1974;301-303.
    • (1974) Nature , vol.250 , pp. 301-303
    • Campbell, J.W.1    Watson, H.C.2    Hodgson, G.I.3
  • 6
    • 0028103275 scopus 로고
    • Collaborative computational project, number 4. The CCP4 suite: Programs for protein crystallography
    • Ccp4
    • CCP4. Collaborative computational project, number 4. The CCP4 suite: programs for protein crystallography. Acta. Crystallog. sect. D. 50:1994;760-763.
    • (1994) Acta. Crystallog. Sect. D , vol.50 , pp. 760-763
  • 7
    • 0031046651 scopus 로고    scopus 로고
    • Protein phosphorylation chain of a Bacillus subtilis fructose-specific phosphotransferase system and its participation in regulation of the expression of the lev operon
    • Charrier V., Deutscher J., Galinier A., Martin-Verstraete M. Protein phosphorylation chain of a Bacillus subtilis fructose-specific phosphotransferase system and its participation in regulation of the expression of the lev operon. Biochemistry. 36:1997;1163-1172.
    • (1997) Biochemistry , vol.36 , pp. 1163-1172
    • Charrier, V.1    Deutscher, J.2    Galinier, A.3    Martin-Verstraete, M.4
  • 8
    • 0026079373 scopus 로고
    • The refined structure of the complex between adenylate kinase from beef heart mitochondrial matrix and its substrate AMP at 1.85 Å resolution
    • Diederichs K., Schulz G. E. The refined structure of the complex between adenylate kinase from beef heart mitochondrial matrix and its substrate AMP at 1.85 Å resolution. J. Mol. Biol. 217:1991;541-549.
    • (1991) J. Mol. Biol. , vol.217 , pp. 541-549
    • Diederichs, K.1    Schulz, G.E.2
  • 10
    • 0022400657 scopus 로고
    • Mancomplex of Escherichia coli
    • Mancomplex of Escherichia coli. J. Biol. Chem. 260:1985;15495-15503.
    • (1985) J. Biol. Chem. , vol.260 , pp. 15495-15503
    • Erni, B.1    Zanolari, B.2
  • 11
    • 0023654528 scopus 로고
    • The mannose permease of Escherichia coli consists of three different proteins. Amino acid sequence and function in sugar transport, sugar phosphorylation, and penetration of phage lambda DNA
    • Erni B., Zanolari Z., Kocher H. P. The mannose permease of Escherichia coli consists of three different proteins. Amino acid sequence and function in sugar transport, sugar phosphorylation, and penetration of phage lambda DNA. J. Biol. Chem. 262:1987;5238-5247.
    • (1987) J. Biol. Chem. , vol.262 , pp. 5238-5247
    • Erni, B.1    Zanolari, Z.2    Kocher, H.P.3
  • 13
    • 0031019983 scopus 로고    scopus 로고
    • Solution structure of the 30 kDa N-terminal domain of enzyme I of the Escherichia coli phosphoenolpyruvate:sugar phosphotransferase system by multidimensional NMR
    • Garrett D. S., Seok Y.-J., Liao D.-I., Peterkofsky A., Gronenborn A. M., Clore G. M. Solution structure of the 30 kDa N-terminal domain of enzyme I of the Escherichia coli phosphoenolpyruvate:sugar phosphotransferase system by multidimensional NMR. Biochemistry. 36:1997;2517-2530.
    • (1997) Biochemistry , vol.36 , pp. 2517-2530
    • Garrett, D.S.1    Seok, Y.-J.2    Liao, D.-I.3    Peterkofsky, A.4    Gronenborn, A.M.5    Clore, G.M.6
  • 14
    • 0026662162 scopus 로고
    • Crystallographic structure of the nitrogenase iron protein from Azotobacter vinelandii
    • Georgiadis M. M., Komiya H., Chakrabarti P., Woo D., Kornuc J. J., Rees D. C. Crystallographic structure of the nitrogenase iron protein from Azotobacter vinelandii. Science. 257:1992;1653-1659.
    • (1992) Science , vol.257 , pp. 1653-1659
    • Georgiadis, M.M.1    Komiya, H.2    Chakrabarti, P.3    Woo, D.4    Kornuc, J.J.5    Rees, D.C.6
  • 15
    • 0031018626 scopus 로고    scopus 로고
    • Secondary structure of the IIB domain of the Escherichia coli mannose transporter, a new fold in the class of α/β twisted open-sheet structures
    • Gschwind R. M., Gemmecker G., Leutner M., Kessler H., Gutknecht R., Lanz R., Flükiger K., Erni B. Secondary structure of the IIB domain of the Escherichia coli mannose transporter, a new fold in the class of α/β twisted open-sheet structures. FEBS Letters. 404:1997;45-50.
    • (1997) FEBS Letters , vol.404 , pp. 45-50
    • Gschwind, R.M.1    Gemmecker, G.2    Leutner, M.3    Kessler, H.4    Gutknecht, R.5    Lanz, R.6    Flükiger, K.7    Erni, B.8
  • 16
    • 0025262173 scopus 로고
    • Selenomethionyl proteins produced for analysis by multiwavelength anomalous diffraction (MAD): A vehicle for direct determination of three-dimensional structure
    • Hendrickson W. A. H., Horton J. R., LeMaster D. M. Selenomethionyl proteins produced for analysis by multiwavelength anomalous diffraction (MAD): a vehicle for direct determination of three-dimensional structure. EMBO J. 9:1990;1665-1672.
    • (1990) EMBO J. , vol.9 , pp. 1665-1672
    • Hendrickson, W.A.H.1    Horton, J.R.2    Lemaster, D.M.3
  • 17
    • 0026483795 scopus 로고
    • An atomic model for protein-protein phosphoryl group transfer
    • Herzberg O. An atomic model for protein-protein phosphoryl group transfer. J. Biol. Chem. 267:1992;24819-24823.
    • (1992) J. Biol. Chem. , vol.267 , pp. 24819-24823
    • Herzberg, O.1
  • 18
    • 0028587898 scopus 로고
    • Unraveling a bacterial hexose transport pathway
    • Herzberg O., Klevit R. Unraveling a bacterial hexose transport pathway. Curr. Opin. Struct. Biol. 4:1994;814-822.
    • (1994) Curr. Opin. Struct. Biol. , vol.4 , pp. 814-822
    • Herzberg, O.1    Klevit, R.2
  • 19
    • 0027991446 scopus 로고
    • The FSSP database of structurally aligned protein fold families
    • Holm L., Sander C. The FSSP database of structurally aligned protein fold families. Nucl. Acids Res. 22:1994;3600-3609.
    • (1994) Nucl. Acids Res. , vol.22 , pp. 3600-3609
    • Holm, L.1    Sander, C.2
  • 20
    • 0029118765 scopus 로고
    • Mechanism of an ATP-dependent carboxylase, dethiobiotin synthetase, based on crystallographic studies of complexes with substrates and a reaction intermediate
    • Huang W., Jia J., Gibson K. J., Taylor W. S., Rendina A. R., Schneider G., Lindqvist Y. Mechanism of an ATP-dependent carboxylase, dethiobiotin synthetase, based on crystallographic studies of complexes with substrates and a reaction intermediate. Biochemistry. 34:1995;10985-10995.
    • (1995) Biochemistry , vol.34 , pp. 10985-10995
    • Huang, W.1    Jia, J.2    Gibson, K.J.3    Taylor, W.S.4    Rendina, A.R.5    Schneider, G.6    Lindqvist, Y.7
  • 21
    • 0029947674 scopus 로고    scopus 로고
    • Membrane topology of the mannose transporter of Escherichia coli K12
    • Huber F., Erni B. Membrane topology of the mannose transporter of Escherichia coli K12. Eur. J. Biochem. 239:1996;810-817.
    • (1996) Eur. J. Biochem. , vol.239 , pp. 810-817
    • Huber, F.1    Erni, B.2
  • 22
    • 0027340388 scopus 로고
    • The 2.0 Å resolution structure of E. coli histidine-containing phosphocarrier protein HPr
    • Jia Z., Quail J. W., Waygood E. B., Delbaere L. T. J. The 2.0 Å resolution structure of E. coli histidine-containing phosphocarrier protein HPr. J. Biol. Chem. 268:1993;22490-22501.
    • (1993) J. Biol. Chem. , vol.268 , pp. 22490-22501
    • Jia, Z.1    Quail, J.W.2    Waygood, E.B.3    Delbaere, L.T.J.4
  • 24
    • 0026244229 scopus 로고
    • MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures
    • Kraulis P. J. MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures. J. Appl. Crystallog. 24:1991;946-950.
    • (1991) J. Appl. Crystallog. , vol.24 , pp. 946-950
    • Kraulis, P.J.1
  • 25
    • 0000243829 scopus 로고
    • PROCHECK: A program to check the stereochemical quality of protein structures
    • Laskowski R. A., MacArthur M. W., Moss D. S., Thornton J. M. PROCHECK: a program to check the stereochemical quality of protein structures. J. Appl. Crystallog. 26:1993;283-291.
    • (1993) J. Appl. Crystallog. , vol.26 , pp. 283-291
    • Laskowski, R.A.1    MacArthur, M.W.2    Moss, D.S.3    Thornton, J.M.4
  • 26
    • 0024284781 scopus 로고
    • NMR sequential assignment of Escherichiacoli thioredoxin utilizing random fractional deuteriation
    • LeMaster D. M., Richards F. M. NMR sequential assignment of Escherichiacoli thioredoxin utilizing random fractional deuteriation. Biochemistry. 27:1988;142-150.
    • (1988) Biochemistry , vol.27 , pp. 142-150
    • Lemaster, D.M.1    Richards, F.M.2
  • 27
    • 0028534956 scopus 로고
    • Enzymes II of the phosphoenolpyruvate-dependent phosphotransferase systems: Their structure and function in carbohydrate transport
    • Lengeler J. W., Jahreis K., Wehmeier U. F. Enzymes II of the phosphoenolpyruvate-dependent phosphotransferase systems: their structure and function in carbohydrate transport. Biochim. Biophys. Acta. 1188:1994;1-28.
    • (1994) Biochim. Biophys. Acta , vol.1188 , pp. 1-28
    • Lengeler, J.W.1    Jahreis, K.2    Wehmeier, U.F.3
  • 29
    • 0030586030 scopus 로고    scopus 로고
    • The first step in sugar transport: Crystal structure of the amino terminal domain of enzyme I of the E. coli PEP: Sugar phosphotransferase system and a model of the phosphotranfer complex with HPr
    • Liao D.-I., Silverton E., Seok Y.-J., Lee B. R., Peterkofsky A., Davies D. R. The first step in sugar transport: crystal structure of the amino terminal domain of enzyme I of the E. coli PEP: sugar phosphotransferase system and a model of the phosphotranfer complex with HPr. Structure. 4:1996;861-872.
    • (1996) Structure , vol.4 , pp. 861-872
    • Liao, D.-I.1    Silverton, E.2    Seok, Y.-J.3    Lee, B.R.4    Peterkofsky, A.5    Davies, D.R.6
  • 30
    • 0029616573 scopus 로고
    • Coupling the phosphotransferase system and the methyl-accepting chemotaxis protein-dependent chemotaxis signaling pathways of Escherichia coli
    • Lux R., Jahreis K., Bettenbrock K., Parkinson J. S., Lengeler J. W. Coupling the phosphotransferase system and the methyl-accepting chemotaxis protein-dependent chemotaxis signaling pathways of Escherichia coli. Proc. Natl Acad. Sci. USA. 92:1995;11583-11587.
    • (1995) Proc. Natl Acad. Sci. USA , vol.92 , pp. 11583-11587
    • Lux, R.1    Jahreis, K.2    Bettenbrock, K.3    Parkinson, J.S.4    Lengeler, J.W.5
  • 31
    • 0028934812 scopus 로고
    • Functional reconstitution of the purified mannose phosphotransferase system of Escherichia coli into phospholipid vesicles
    • Mao Q., Schunk T., Flükiger K., Erni B. Functional reconstitution of the purified mannose phosphotransferase system of Escherichia coli into phospholipid vesicles. J. Biol. Chem. 270:1995;5258-5265.
    • (1995) J. Biol. Chem. , vol.270 , pp. 5258-5265
    • Mao, Q.1    Schunk, T.2    Flükiger, K.3    Erni, B.4
  • 32
    • 0025142206 scopus 로고
    • Levanase operon of Bacillus subtillis includes a fructose-specific phosphotransferase system regulating the expression of the operon
    • Martin-Verstraete I., Debarbouille M., Klier A., Rapoport G. Levanase operon of Bacillus subtillis includes a fructose-specific phosphotransferase system regulating the expression of the operon. J. Mol. Biol. 214:1990;657-671.
    • (1990) J. Mol. Biol. , vol.214 , pp. 657-671
    • Martin-Verstraete, I.1    Debarbouille, M.2    Klier, A.3    Rapoport, G.4
  • 33
    • 0028579433 scopus 로고
    • Protein structural similarities predicted by sequence-structure compatibility method
    • Matsuo Y., Nishikawa K. Protein structural similarities predicted by sequence-structure compatibility method. Protein Sci. 3:1994;2055-2063.
    • (1994) Protein Sci. , vol.3 , pp. 2055-2063
    • Matsuo, Y.1    Nishikawa, K.2
  • 34
    • 0028057108 scopus 로고
    • Raster3D version 2.0. A program for photorealistic molecular graphics
    • Merritt E. A., Murphy M. E. P. Raster3D version 2.0. A program for photorealistic molecular graphics. Acta Crystallog. sect. D. 50:1994;869-873.
    • (1994) Acta Crystallog. Sect. D , vol.50 , pp. 869-873
    • Merritt, E.A.1    Murphy, M.E.P.2
  • 35
    • 0027112289 scopus 로고
    • 1.7 Å X-ray structure of the periplasmic ribose receptor from Escherichia coli
    • Mowbray S. L., Cole L. B. 1.7 Å X-ray structure of the periplasmic ribose receptor from Escherichia coli. J. Mol. Biol. 225:1992;155-175.
    • (1992) J. Mol. Biol. , vol.225 , pp. 155-175
    • Mowbray, S.L.1    Cole, L.B.2
  • 36
    • 0028961335 scopus 로고
    • SCOP: A structural classification of proteins. Database for the investigation of sequences and structures
    • Murzin A. G., Brenner S. E., Hubbard T., Chothia C. SCOP: a structural classification of proteins. Database for the investigation of sequences and structures. J. Mol. Biol. 247:1995;536-540.
    • (1995) J. Mol. Biol. , vol.247 , pp. 536-540
    • Murzin, A.G.1    Brenner, S.E.2    Hubbard, T.3    Chothia, C.4
  • 37
    • 0026458015 scopus 로고
    • Transport proteins in bacteria: Common themes in their design
    • Nikaido H., Saier M. H. J. Transport proteins in bacteria: common themes in their design. Science. 258:1992;936-942.
    • (1992) Science , vol.258 , pp. 936-942
    • Nikaido, H.1    Saier, M.H.J.2
  • 39
    • 0002634621 scopus 로고
    • Maximum likelihood refinement of heavy atom parameters
    • W. Wolf, P.R. Evans, & A.G.W. Leslie. Warrington: SERC Daresbury Laboratory
    • Otwinowski Z. Maximum likelihood refinement of heavy atom parameters. Wolf W., Evans P. R., Leslie A. G. W. Isomorphous Replacement and Anomalous Scattering. 1991;80-86 SERC Daresbury Laboratory, Warrington.
    • (1991) Isomorphous Replacement and Anomalous Scattering , pp. 80-86
    • Otwinowski, Z.1
  • 40
    • 0027291428 scopus 로고
    • Phosphoenolpyruvate: Carbohydrate phosphotransferase systems of bacteria
    • Postma P. W., Lengeler J. W., Jacobson G. R. Phosphoenolpyruvate: carbohydrate phosphotransferase systems of bacteria. Microbiol. Rev. 57:1993;543-594.
    • (1993) Microbiol. Rev. , vol.57 , pp. 543-594
    • Postma, P.W.1    Lengeler, J.W.2    Jacobson, G.R.3
  • 42
    • 0028589065 scopus 로고
    • Structural consequences of histidine phosphorylation: NMR characterization of the phosphohistidine form of histidine-containing protein from Bacillus subtilis and Escherichia coli
    • Rajagopal P., Waygood E. B., Klevit R. E. Structural consequences of histidine phosphorylation: NMR characterization of the phosphohistidine form of histidine-containing protein from Bacillus subtilis and Escherichia coli. Biochemistry. 33:1994;15271-15282.
    • (1994) Biochemistry , vol.33 , pp. 15271-15282
    • Rajagopal, P.1    Waygood, E.B.2    Klevit, R.E.3
  • 43
    • 0028104094 scopus 로고
    • The bacterial phosphotransferase system: New frontiers 30 years later
    • Saier M. H. J., Reizer J. The bacterial phosphotransferase system: new frontiers 30 years later. Mol. Microbiol. 13:1994;755-764.
    • (1994) Mol. Microbiol. , vol.13 , pp. 755-764
    • Saier, M.H.J.1    Reizer, J.2
  • 46
    • 0030612122 scopus 로고    scopus 로고
    • lactosefrom Lactococcus lactis reveals a new fold and points to possible interactions of a multicomponent system
    • lactosefrom Lactococcus lactis reveals a new fold and points to possible interactions of a multicomponent system. Structure. 5:1997;775-788.
    • (1997) Structure , vol.5 , pp. 775-788
    • Sliz, P.1    Engelmann, R.2    Hengstenberg, W.3    Pai, E.F.4
  • 47
    • 0021358542 scopus 로고
    • +-derivatives of Escherichia coli K-12 and chemotaxis towards sorbose
    • +-derivatives of Escherichia coli K-12 and chemotaxis towards sorbose. J. Bacteriol. 157:1984;39-45.
    • (1984) J. Bacteriol. , vol.157 , pp. 39-45
    • Sprenger, G.A.1    Lengeler, J.W.2
  • 51
    • 0028905499 scopus 로고
    • The high-resolution structure of the phosphorylated form of the histidine-containing phosphocarrier protein HPr from E. coli determined by restrained molecular dynamics from nuclear magnetic resonance nuclear Overhauser effect data
    • Van Nuland N. A. J., Boelens R., Scheek R. M., Robillard G. T. The high-resolution structure of the phosphorylated form of the histidine-containing phosphocarrier protein HPr from E. coli determined by restrained molecular dynamics from nuclear magnetic resonance nuclear Overhauser effect data. J. Mol. Biol. 246:1995;180-193.
    • (1995) J. Mol. Biol. , vol.246 , pp. 180-193
    • Van Nuland, N.A.J.1    Boelens, R.2    Scheek, R.M.3    Robillard, G.T.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.