메뉴 건너뛰기




Volumn 4, Issue 5, 1997, Pages 405-412

Oligosaccharide substrate binding in Escherichia coli maltodextrin phosphorylase

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL PROTEIN; BINDING PROTEIN; CARBOHYDRATE BINDING PROTEIN; MALTODEXTRIN; OLIGOSACCHARIDE; PHOSPHORYLASE;

EID: 0030890246     PISSN: 10728368     EISSN: None     Source Type: Journal    
DOI: 10.1038/nsb0597-405     Document Type: Article
Times cited : (59)

References (42)
  • 1
    • 0022555847 scopus 로고
    • Carbohydrate binding proteins: Tertiary structures and protein sugar interactions
    • Quiocho, F.A. Carbohydrate binding proteins: tertiary structures and protein sugar interactions. Ann. Rev. Biochem. 55, 287-315 (1986).
    • (1986) Ann. Rev. Biochem. , vol.55 , pp. 287-315
    • Quiocho, F.A.1
  • 2
    • 0024220313 scopus 로고
    • Protein-oligosaccharide interactions: Lysozyme, phosphorylase, amylases
    • Johnson, L.N. et al. Protein-oligosaccharide interactions: lysozyme, phosphorylase, amylases. Curr. Topics Microbiol. Immunol. 139, 81-134 (1988).
    • (1988) Curr. Topics Microbiol. Immunol. , vol.139 , pp. 81-134
    • Johnson, L.N.1
  • 3
    • 12944260514 scopus 로고
    • Atomic features of protein-carbohydrate interactions
    • Vyas, N.K. Atomic features of protein-carbohydrate interactions. Curr. Opin. Struct. Biol. 1, 732-740 (1991).
    • (1991) Curr. Opin. Struct. Biol. , vol.1 , pp. 732-740
    • Vyas, N.K.1
  • 4
    • 0029952519 scopus 로고    scopus 로고
    • Structural basis of lectin-carbohydrate recognition
    • Weiss, W.I. & Drickamer, K. Structural basis of lectin-carbohydrate recognition. Ann. Rev. Biochem. 65, 441-473 (1996).
    • (1996) Ann. Rev. Biochem. , vol.65 , pp. 441-473
    • Weiss, W.I.1    Drickamer, K.2
  • 5
    • 0028198814 scopus 로고
    • The active centre of a mammalian α-amylase. Structure of the complex of a pancreatic α-amylase with a carbohydrate inhibitor refined to 2.2Å resolution
    • Qian, M., Haser, R., Buisson, G., Duee, E. & Payan, F. The active centre of a mammalian α-amylase. Structure of the complex of a pancreatic α-amylase with a carbohydrate inhibitor refined to 2.2Å resolution. Biochemistry 33, 6284-6294 (1994).
    • (1994) Biochemistry , vol.33 , pp. 6284-6294
    • Qian, M.1    Haser, R.2    Buisson, G.3    Duee, E.4    Payan, F.5
  • 6
    • 0030584665 scopus 로고    scopus 로고
    • The crystal structure of endoglucanase CelA, a family 8 glycosl hydrolase from Clostridium thermocellum
    • Alzari, P.M., Souchon, H. & Dominguez, R. The crystal structure of endoglucanase CelA, a family 8 glycosl hydrolase from Clostridium thermocellum. Structure 4, 265-275 (1996).
    • (1996) Structure , vol.4 , pp. 265-275
    • Alzari, P.M.1    Souchon, H.2    Dominguez, R.3
  • 7
    • 0029644059 scopus 로고    scopus 로고
    • Crystal structure of various maltooligosaccharides bound to maltoporin reveal a specific sugar translocation pathway
    • Dutzler, R., Wang, Y.-F., Rizkallah, P.J., Rosenbusch, J.P. & Schirmer, T. Crystal structure of various maltooligosaccharides bound to maltoporin reveal a specific sugar translocation pathway. Structure 4, 127-134 (1996).
    • (1996) Structure , vol.4 , pp. 127-134
    • Dutzler, R.1    Wang, Y.-F.2    Rizkallah, P.J.3    Rosenbusch, J.P.4    Schirmer, T.5
  • 8
    • 0029117927 scopus 로고
    • The CH/π interaction significance in molecular recognition
    • Nishio, M., Umezawa, Y., Hirota, M. & Takeuchi, Y. The CH/π interaction significance in molecular recognition. Tetrahedron 51, 8665-8701 (1995).
    • (1995) Tetrahedron , vol.51 , pp. 8665-8701
    • Nishio, M.1    Umezawa, Y.2    Hirota, M.3    Takeuchi, Y.4
  • 9
    • 0025217008 scopus 로고
    • The refined crystal structure of the phosphorylase-heptulose 2-phosphate-oligosaccharide-AMP complex
    • Johnson, L.N., Acharya, K.R., Jordan, M.D. & McLaughlin, P.J. The refined crystal structure of the phosphorylase-heptulose 2-phosphate-oligosaccharide-AMP complex. J. Mol. Biol. 211, 645-661 (1990).
    • (1990) J. Mol. Biol. , vol.211 , pp. 645-661
    • Johnson, L.N.1    Acharya, K.R.2    Jordan, M.D.3    McLaughlin, P.J.4
  • 10
    • 0025598298 scopus 로고
    • Comparison of the binding of glucose and glucose-1-phosphate derivatives to T state glycogen phosphorylase b
    • Martin, J.L., Withers, S.G. & Johnson, L.N. Comparison of the binding of glucose and glucose-1-phosphate derivatives to T state glycogen phosphorylase b. Biochemistry 29, 10745-10757 (1990).
    • (1990) Biochemistry , vol.29 , pp. 10745-10757
    • Martin, J.L.1    Withers, S.G.2    Johnson, L.N.3
  • 11
    • 0024322304 scopus 로고
    • The allosteric transition of glycogen phosphorylase
    • Barford, D. & Johnson, L.N. The allosteric transition of glycogen phosphorylase. Nature 340, 609-614 (1989).
    • (1989) Nature , vol.340 , pp. 609-614
    • Barford, D.1    Johnson, L.N.2
  • 12
    • 0026033985 scopus 로고
    • The structural mechanism for glycogen phosphorylase control by phosphorylation and by AMP
    • Barford, D., Hu, S.-H. & Johnson, L.N. The structural mechanism for glycogen phosphorylase control by phosphorylation and by AMP. J. Mol. Biol. 218, 233-260 (1991).
    • (1991) J. Mol. Biol. , vol.218 , pp. 233-260
    • Barford, D.1    Hu, S.-H.2    Johnson, L.N.3
  • 14
    • 0017891664 scopus 로고
    • X-ray crystallographic and kinetic studies of oligosaccharide binding to phosphorylase
    • Kasvinsky, P., Madsen, N.B., Fletterick, R.J. & Sygusch, J. X-ray crystallographic and kinetic studies of oligosaccharide binding to phosphorylase. J. Biol. Chem. 253, 1290-1296 (1978).
    • (1978) J. Biol. Chem. , vol.253 , pp. 1290-1296
    • Kasvinsky, P.1    Madsen, N.B.2    Fletterick, R.J.3    Sygusch, J.4
  • 15
    • 0016794896 scopus 로고
    • Kinetics of glycogen phosphorylase a with a series of semisynthetic, branched saccharides: A model for binding of polysaccharide substrates
    • Hu, H.-Y. & Gold, A.M. Kinetics of glycogen phosphorylase a with a series of semisynthetic, branched saccharides: a model for binding of polysaccharide substrates. Biochemistry 14, 2224-2230 (1975).
    • (1975) Biochemistry , vol.14 , pp. 2224-2230
    • Hu, H.-Y.1    Gold, A.M.2
  • 16
    • 0023283774 scopus 로고
    • Catalysis in the crystal: Synchrotron radiation studies with glycogen phosphorylase b
    • Hajdu, J. et al. Catalysis in the crystal: synchrotron radiation studies with glycogen phosphorylase b. EMBO J. 6, 539-546 (1987).
    • (1987) EMBO J. , vol.6 , pp. 539-546
    • Hajdu, J.1
  • 17
    • 0021668178 scopus 로고
    • Positive control of transcription initiation in bacteria
    • Raibaud, O. & Schwartz, M. Positive control of transcription initiation in bacteria. Ann. Rev. Genet. 18, 207-231 (1984).
    • (1984) Ann. Rev. Genet. , vol.18 , pp. 207-231
    • Raibaud, O.1    Schwartz, M.2
  • 18
    • 0014133549 scopus 로고
    • La maltodextrine phosphorylase d'Escherichia coli
    • Schwartz, M. & Hofnung, M. La maltodextrine phosphorylase d'Escherichia coli. Eur. J. Biochem. 2, 132-145 (1967).
    • (1967) Eur. J. Biochem. , vol.2 , pp. 132-145
    • Schwartz, M.1    Hofnung, M.2
  • 19
    • 0021964124 scopus 로고
    • Evolution of catalytic and regulatory sites in phosphorylase
    • Palm, D., Goerl, R. & Burger, K.J. Evolution of catalytic and regulatory sites in phosphorylase. Nature 313, 500-502 (1985).
    • (1985) Nature , vol.313 , pp. 500-502
    • Palm, D.1    Goerl, R.2    Burger, K.J.3
  • 20
    • 0028954290 scopus 로고
    • A study of binary complexes of Escherichia coli maltodextrin phosphorylase; α-D-glucose 1-methylenephosphonate as a probe of pyridoxal 5′-phosphate-substrate interactions
    • Becker, S., Schnackerz, K.D. & Schinzel, R. A study of binary complexes of Escherichia coli maltodextrin phosphorylase; α-D-glucose 1-methylenephosphonate as a probe of pyridoxal 5′-phosphate-substrate interactions. Biochim. Biophys. Acta 1243, 381-385 (1994).
    • (1994) Biochim. Biophys. Acta , vol.1243 , pp. 381-385
    • Becker, S.1    Schnackerz, K.D.2    Schinzel, R.3
  • 21
    • 0028822343 scopus 로고
    • Structures of oligosaccharide-bound forms of the endoglucanas V from Humicola insolens at 1.9Å resolution
    • Davies, G.D., Tolley, S.P., Henrissat, B., Hjort, C. & Schulein, M. Structures of oligosaccharide-bound forms of the endoglucanas V from Humicola insolens at 1.9Å resolution. Biochemistry 34, 16210-16220 (1995).
    • (1995) Biochemistry , vol.34 , pp. 16210-16220
    • Davies, G.D.1    Tolley, S.P.2    Henrissat, B.3    Hjort, C.4    Schulein, M.5
  • 22
    • 0031014875 scopus 로고    scopus 로고
    • The crystal structure of E. coli maltodextrin phosphorylase provides an explanation for the activity without control in this basic archetype of a phosphorylase
    • Watson, K.A., Schinzel, R., Palm, D. & Johnson, L.N. The crystal structure of E. coli maltodextrin phosphorylase provides an explanation for the activity without control in this basic archetype of a phosphorylase. EMBO J. 16, 1-14 (1997).
    • (1997) EMBO J. , vol.16 , pp. 1-14
    • Watson, K.A.1    Schinzel, R.2    Palm, D.3    Johnson, L.N.4
  • 24
    • 0029944134 scopus 로고    scopus 로고
    • Mutational analysis of the oligosaccharide recognition site at the active site of Escherichia coli maltodextrin phosphorylase
    • Drueckes, P., Boeck, B., Palm, D. & Schinzel, R. Mutational analysis of the oligosaccharide recognition site at the active site of Escherichia coli maltodextrin phosphorylase. Biochemistry 35, 6727-6734 (1996).
    • (1996) Biochemistry , vol.35 , pp. 6727-6734
    • Drueckes, P.1    Boeck, B.2    Palm, D.3    Schinzel, R.4
  • 25
    • 0027071836 scopus 로고
    • The molecular mechanism for the tetrameric association of glycogen phosphorylase promoted by protein phosphorylation
    • Barford, D. & Johnson, L.N. The molecular mechanism for the tetrameric association of glycogen phosphorylase promoted by protein phosphorylation. Protein Sci. 1, 472-493 (1992).
    • (1992) Protein Sci. , vol.1 , pp. 472-493
    • Barford, D.1    Johnson, L.N.2
  • 26
    • 0014963088 scopus 로고
    • Control of phosphorylase in the glycogen particle. I. Isolation and characterisation of the protein glycogen complex
    • Meyer, F., Heilmeyer, L.M.G., Hashke, R.H. & Fischer, E.H. Control of phosphorylase in the glycogen particle. I. Isolation and characterisation of the protein glycogen complex. J. Biol. Chem. 245, 6642-6648 (1970).
    • (1970) J. Biol. Chem. , vol.245 , pp. 6642-6648
    • Meyer, F.1    Heilmeyer, L.M.G.2    Hashke, R.H.3    Fischer, E.H.4
  • 27
    • 0002857875 scopus 로고
    • Glycogen phosphorylase b
    • ed. Herve, G. CRC Press, Boca Raton, Florida
    • Johnson, L.N. et al. Glycogen phosphorylase b. in Allosteric Enzymes (ed. Herve, G.) 81-127 (CRC Press, Boca Raton, Florida, 1989).
    • (1989) Allosteric Enzymes , pp. 81-127
    • Johnson, L.N.1
  • 28
    • 0029953209 scopus 로고    scopus 로고
    • Ternary complex crystal structures of glycogen phosphorylase with a transition state analogue nojirimycin tetrazole and phosphate in the T and R states
    • Mitchell, E.P. et al. Ternary complex crystal structures of glycogen phosphorylase with a transition state analogue nojirimycin tetrazole and phosphate in the T and R states. Biochemistry 35, 7341-7355 (1996).
    • (1996) Biochemistry , vol.35 , pp. 7341-7355
    • Mitchell, E.P.1
  • 29
    • 37049126855 scopus 로고
    • Polysaccharide conformation. Part IX. Monte Carlo calculation of conformational energies for disaccharides and comparison with experiment
    • Rees, D.A. & Smith, P.J.C Polysaccharide conformation. Part IX. Monte Carlo calculation of conformational energies for disaccharides and comparison with experiment. J. Chem. Soc. Perkin II, 836-840 (1975).
    • (1975) J. Chem. Soc. Perkin II , pp. 836-840
    • Rees, D.A.1    Smith, P.J.C.2
  • 30
    • 0028181134 scopus 로고
    • Crystal structures of Soybean β-amylase reacted with β-maltose and maltal: Active site components and their apparent roles in catalysis
    • Mikami, B., Degano, M., Hehre, E.J. & Sacchettinin, J.C. Crystal structures of Soybean β-amylase reacted with β-maltose and maltal: active site components and their apparent roles in catalysis. Biochemistry 33, 7779-7787 (1994).
    • (1994) Biochemistry , vol.33 , pp. 7779-7787
    • Mikami, B.1    Degano, M.2    Hehre, E.J.3    Sacchettinin, J.C.4
  • 31
    • 0030593488 scopus 로고    scopus 로고
    • Carbohydrate and protein-based inhibitors of porcine pancreatic α-amylase: Structure analysis and comparison of their binding characteristics
    • Machius, M., Vertesy, L., Huber, R. & Wiegland, G. Carbohydrate and protein-based inhibitors of porcine pancreatic α-amylase: structure analysis and comparison of their binding characteristics. J. Mol. Biol. 260, 409-421 (1996).
    • (1996) J. Mol. Biol. , vol.260 , pp. 409-421
    • Machius, M.1    Vertesy, L.2    Huber, R.3    Wiegland, G.4
  • 32
    • 0023762144 scopus 로고
    • Channels at the catalytic site of glycogen phosphorylase b: Binding and kinetic studies with the β-glycosidase inhibitor D-gluconohydroximo-1,5-lactone N-phenylurethane
    • Barford, D. et al. Channels at the catalytic site of glycogen phosphorylase b: binding and kinetic studies with the β-glycosidase inhibitor D-gluconohydroximo-1,5-lactone N-phenylurethane. Biochemistry 27, 6733-6741 (1988).
    • (1988) Biochemistry , vol.27 , pp. 6733-6741
    • Barford, D.1
  • 33
    • 0027018077 scopus 로고
    • Catalytic mechanism of glycogen phosphorylase
    • Johnson, L.N., Hu, S.-H. & Barford, D. Catalytic mechanism of glycogen phosphorylase. Faraday Disc. 93, 131-142 (1992).
    • (1992) Faraday Disc. , vol.93 , pp. 131-142
    • Johnson, L.N.1    Hu, S.-H.2    Barford, D.3
  • 34
    • 0025017865 scopus 로고
    • The role of pyridoxal-5′-phosphate in glycogen phosphorylase catalysis
    • Palm, D., Klein, H.W., Schinzel, R., Buehner, M. & Helmreich, E.J.M. The role of pyridoxal-5′-phosphate in glycogen phosphorylase catalysis. Biochemistry 29, 1099-1107 (1990).
    • (1990) Biochemistry , vol.29 , pp. 1099-1107
    • Palm, D.1    Klein, H.W.2    Schinzel, R.3    Buehner, M.4    Helmreich, E.J.M.5
  • 35
    • 0002452464 scopus 로고
    • DENZO
    • eds Sawyer, L., Isaacs, N. & Bailey, S. SERC Laboratory , Daresbury, Warrington, UK. DL/SC1/R34
    • Otwinowski, Z. DENZO. in Data Collection and Processing. (eds Sawyer, L., Isaacs, N. & Bailey, S.) 56-62 , SERC Laboratory , Daresbury, Warrington, UK. DL/SC1/R34, 1993).
    • (1993) Data Collection and Processing , pp. 56-62
    • Otwinowski, Z.1
  • 36
    • 0028103275 scopus 로고
    • The CCP4 (Collaborative Computational Project Number 4) suite: Programmes for protein crystallography
    • CCP4. The CCP4 (Collaborative Computational Project Number 4) suite: programmes for protein crystallography. Acta Crystallogr. D50, 760-763 (1994).
    • (1994) Acta Crystallogr. , vol.D50 , pp. 760-763
  • 37
    • 84920325457 scopus 로고
    • AMoRe: An automated package for molecular replacement
    • Navaza, J. AMoRe: an automated package for molecular replacement. Acta Crystallogr. A50, 157-163 (1990).
    • (1990) Acta Crystallogr. , vol.A50 , pp. 157-163
    • Navaza, J.1
  • 39
    • 79952608525 scopus 로고
    • Accurate bond length and angle parameters for X-ray protein structure refinement
    • Engh, R.A. & Huber, R. Accurate bond length and angle parameters for X-ray protein structure refinement. Acta Crystallogr. A47, 392-400 (1991).
    • (1991) Acta Crystallogr. , vol.A47 , pp. 392-400
    • Engh, R.A.1    Huber, R.2
  • 41
    • 84889120137 scopus 로고
    • Improved methods for building protein models in electron density maps and location of errors in these models
    • Jones, T.A., Zou, J.-Y., Cowan, S.W. & Kjeldgaard, M. Improved methods for building protein models in electron density maps and location of errors in these models. Acta Crystallogr. A47, 110-119 (1991).
    • (1991) Acta Crystallogr. , vol.A47 , pp. 110-119
    • Jones, T.A.1    Zou, J.-Y.2    Cowan, S.W.3    Kjeldgaard, M.4
  • 42
    • 0024520745 scopus 로고
    • Site-directed mutagenesis by overlap extension using the polymerase chain reaction
    • Ho, S.N., Hunt, H.D., Horton, R.M., Pullen, J.K. & Pease, L. Site-directed mutagenesis by overlap extension using the polymerase chain reaction. Gene 77, 51-59 (1989).
    • (1989) Gene , vol.77 , pp. 51-59
    • Ho, S.N.1    Hunt, H.D.2    Horton, R.M.3    Pullen, J.K.4    Pease, L.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.