메뉴 건너뛰기




Volumn 23, Issue 16, 2004, Pages 3196-3205

Crystal structure of glycogen synthase: Homologous enzymes catalyze glycogen synthesis and degradation

Author keywords

Glycogen; Glycosyltransferase; Starch 3D structure; X ray crystallography

Indexed keywords

ADENOSINE PHOSPHATE; GLUCAN 1,4 ALPHA GLUCOSIDASE; GLYCOGEN SYNTHASE; STARCH;

EID: 4444373841     PISSN: 02614189     EISSN: None     Source Type: Journal    
DOI: 10.1038/sj.emboj.7600324     Document Type: Article
Times cited : (147)

References (49)
  • 3
    • 0034012439 scopus 로고    scopus 로고
    • Control of glycogen synthesis is shared between glucose transport and glycogen synthase in skeletal muscle fibers
    • Azpiazu I, Manchester J, Skurat AV, Roach PJ, Lawrence JC (2000) Control of glycogen synthesis is shared between glucose transport and glycogen synthase in skeletal muscle fibers. Am J Physiol Endocrinol Metab 278: E234-E243
    • (2000) Am J Physiol Endocrinol Metab , vol.278
    • Azpiazu, I.1    Manchester, J.2    Skurat, A.V.3    Roach, P.J.4    Lawrence, J.C.5
  • 4
    • 0142040430 scopus 로고    scopus 로고
    • From bacterial glycogen to starch: Understanding the biogenesis of the plant starch granule
    • Ball S, Morell MK (2003) From bacterial glycogen to starch: understanding the biogenesis of the plant starch granule. Annu Rev Plant Biol 54: 207-233
    • (2003) Annu Rev Plant Biol , vol.54 , pp. 207-233
    • Ball, S.1    Morell, M.K.2
  • 5
    • 0024322304 scopus 로고
    • The allosteric transition of glycogen phosphorylase
    • Barford D, Johnson LN (1989) The allosteric transition of glycogen phosphorylase. Nature 340: 609-616
    • (1989) Nature , vol.340 , pp. 609-616
    • Barford, D.1    Johnson, L.N.2
  • 6
    • 0242460576 scopus 로고    scopus 로고
    • Generation, representation and flow of phase information in structure determination: Recent developments in and around SHARP 2.0
    • Bricogne G, Vonrhein C, Flensburg C, Schiltz M, Paciorek W (2003) Generation, representation and flow of phase information in structure determination: recent developments in and around SHARP 2.0. Acta Crystallogr D 59: 2023-2030
    • (2003) Acta Crystallogr D , vol.59 , pp. 2023-2030
    • Bricogne, G.1    Vonrhein, C.2    Flensburg, C.3    Schiltz, M.4    Paciorek, W.5
  • 9
    • 0020479563 scopus 로고
    • Rabbit liver glycogen synthase. Susceptibility of the enzyme subunit to proteolysis
    • Camici M, DePaoli-Roach AA, Roach PJ (1982) Rabbit liver glycogen synthase. Susceptibility of the enzyme subunit to proteolysis. J Biol Chem 257: 9898-9901
    • (1982) J Biol Chem , vol.257 , pp. 9898-9901
    • Camici, M.1    DePaoli-Roach, A.A.2    Roach, P.J.3
  • 10
    • 0033580656 scopus 로고    scopus 로고
    • Structure of the nucleotide-diphospho-sugar transferase, SpsA from Bacillus subtilis, in native and nucleotide-complexed forms
    • Charnock SJ, Davies GJ (1999) Structure of the nucleotide-diphospho-sugar transferase, SpsA from Bacillus subtilis, in native and nucleotide-complexed forms. Biochemistry 38: 6380-6385
    • (1999) Biochemistry , vol.38 , pp. 6380-6385
    • Charnock, S.J.1    Davies, G.J.2
  • 11
    • 0028103275 scopus 로고
    • The CCP4 suite: Programs for protein crystallography
    • Collaborative Computational Project Number 4 (1994) The CCP4 suite: programs for protein crystallography. Acta Crystallogr D 50: 760-763
    • (1994) Acta Crystallogr D , vol.50 , pp. 760-763
  • 12
    • 0037466315 scopus 로고    scopus 로고
    • An evolving hierarchical family classification for glycosyltransferases
    • Coutinho PM, Deleury E, Davies GJ, Henrissat B (2003) An evolving hierarchical family classification for glycosyltransferases. J Mol Biol 328: 307-317
    • (2003) J Mol Biol , vol.328 , pp. 307-317
    • Coutinho, P.M.1    Deleury, E.2    Davies, G.J.3    Henrissat, B.4
  • 13
    • 0028822343 scopus 로고
    • Structures of oligosaccharide-bound forms of the endoglucanase V from Humicola insolens at 1.9 Å resolution
    • Davies GJ, Tolley SP, Henrissat B, Hjort C, Schulein M (1995) Structures of oligosaccharide-bound forms of the endoglucanase V from Humicola insolens at 1.9 Å resolution. Biochemistry 34: 16210-16220
    • (1995) Biochemistry , vol.34 , pp. 16210-16220
    • Davies, G.J.1    Tolley, S.P.2    Henrissat, B.3    Hjort, C.4    Schulein, M.5
  • 14
    • 0025078378 scopus 로고
    • Identification of lysine 15 at the active site in Escherichia coli glycogen synthase. Conservation of Lys-X-Gly-Gly sequence in the bacterial and mammalian enzymes
    • Furukawa K, Tagaya M, Inouye M, Preiss J, Fukui T (1990) Identification of lysine 15 at the active site in Escherichia coli glycogen synthase. Conservation of Lys-X-Gly-Gly sequence in the bacterial and mammalian enzymes. J Biol Chem 265: 2086-2090
    • (1990) J Biol Chem , vol.265 , pp. 2086-2090
    • Furukawa, K.1    Tagaya, M.2    Inouye, M.3    Preiss, J.4    Fukui, T.5
  • 15
    • 0027524850 scopus 로고
    • Role of the conserved Lys-X-Gly-Gly sequence at the ADP-glucose-binding site in Escherichia coli glycogen synthase
    • Furukawa K, Tagaya M, Tanizawa K, Fukui T (1993) Role of the conserved Lys-X-Gly-Gly sequence at the ADP-glucose-binding site in Escherichia coli glycogen synthase. J Biol Chem 268: 23837-23842
    • (1993) J Biol Chem , vol.268 , pp. 23837-23842
    • Furukawa, K.1    Tagaya, M.2    Tanizawa, K.3    Fukui, T.4
  • 16
    • 0028174042 scopus 로고
    • Identification of Lys277 at the active site of Escherichia coli glycogen synthase. Application of affinity labeling combined with site-directed mutagenesis
    • Furukawa K, Tagaya M, Tanizawa K, Fukui T (1994) Identification of Lys277 at the active site of Escherichia coli glycogen synthase. Application of affinity labeling combined with site-directed mutagenesis. J Biol Chem 269: 868-871
    • (1994) J Biol Chem , vol.269 , pp. 868-871
    • Furukawa, K.1    Tagaya, M.2    Tanizawa, K.3    Fukui, T.4
  • 17
    • 0036384359 scopus 로고    scopus 로고
    • Enzymatic catalysis in crystals of Escherichia coli maltodextrin phosphorylase
    • Geremia S, Campagnolo M, Schinzel R, Johnson LN (2002) Enzymatic catalysis in crystals of Escherichia coli maltodextrin phosphorylase. J Mol Biol 322: 413-423
    • (2002) J Mol Biol , vol.322 , pp. 413-423
    • Geremia, S.1    Campagnolo, M.2    Schinzel, R.3    Johnson, L.N.4
  • 18
    • 0036307824 scopus 로고    scopus 로고
    • Crystal structure of the autocatalytic initiator of glycogen biosynthesis, glycogenin
    • Gibbons BJ, Roach PJ, Hurley TD (2002) Crystal structure of the autocatalytic initiator of glycogen biosynthesis, glycogenin. J Mol Biol 319: 463-477
    • (2002) J Mol Biol , vol.319 , pp. 463-477
    • Gibbons, B.J.1    Roach, P.J.2    Hurley, T.D.3
  • 19
    • 0345826092 scopus 로고    scopus 로고
    • The donor subsite of trehalose-6-phosphate synthase: Binary complexes with UDP-glucose and UDP-2-deoxy-2-fluoro-glucose at 2 Å resolution
    • Gibson RP, Tarling CA, Roberts S, Withers SG, Davies GJ (2004) The donor subsite of trehalose-6-phosphate synthase: binary complexes with UDP-glucose and UDP-2-deoxy-2-fluoro-glucose at 2 Å resolution. J Biol Chem 279: 1950-1955
    • (2004) J Biol Chem , vol.279 , pp. 1950-1955
    • Gibson, R.P.1    Tarling, C.A.2    Roberts, S.3    Withers, S.G.4    Davies, G.J.5
  • 20
    • 0036909547 scopus 로고    scopus 로고
    • Insights into trehalose synthesis provided by the structure of the retaining glucosyltransferase OtsA
    • Gibson RP, Turkenburg JP, Charnock SJ, Lloyd R, Davies GJ (2002) Insights into trehalose synthesis provided by the structure of the retaining glucosyltransferase OtsA. Chem Biol 9: 1337-1346
    • (2002) Chem Biol , vol.9 , pp. 1337-1346
    • Gibson, R.P.1    Turkenburg, J.P.2    Charnock, S.J.3    Lloyd, R.4    Davies, G.J.5
  • 21
  • 22
    • 0037082107 scopus 로고    scopus 로고
    • Mutations of muscle glycogen synthase that disable activation by glucose 6-phosphate
    • Hanashiro I, Roach PJ (2002) Mutations of muscle glycogen synthase that disable activation by glucose 6-phosphate. Arch Biochem Biophys 397: 286-292
    • (2002) Arch Biochem Biophys , vol.397 , pp. 286-292
    • Hanashiro, I.1    Roach, P.J.2
  • 23
    • 0027436392 scopus 로고
    • Control of yeast glycogen synthase-2 by COOH-terminal phosphorylation
    • Hardy TA, Roach PJ (1993) Control of yeast glycogen synthase-2 by COOH-terminal phosphorylation. J Biol Chem 268: 23799-23805
    • (1993) J Biol Chem , vol.268 , pp. 23799-23805
    • Hardy, T.A.1    Roach, P.J.2
  • 24
    • 0036716927 scopus 로고    scopus 로고
    • Glycogen metabolism loss: A common marker of parasitic behaviour in bacteria?
    • Henrissat B, Deleury E, Coutinho PM (2002) Glycogen metabolism loss: a common marker of parasitic behaviour in bacteria? Trends Genet 18: 437-440
    • (2002) Trends Genet , vol.18 , pp. 437-440
    • Henrissat, B.1    Deleury, E.2    Coutinho, P.M.3
  • 25
    • 0028969335 scopus 로고
    • Evolutionary link between glycogen phosphorylase and a DNA modifying enzyme
    • Holm L, Sander C (1995) Evolutionary link between glycogen phosphorylase and a DNA modifying enzyme. EMBO J 14: 1287-1293
    • (1995) EMBO J , vol.14 , pp. 1287-1293
    • Holm, L.1    Sander, C.2
  • 26
    • 0037423706 scopus 로고    scopus 로고
    • Three-dimensional structure and substrate binding of Bacillus stearothermophilus neopullulanase
    • Hondoh H, Kuriki T, Matsuura Y (2003) Three-dimensional structure and substrate binding of Bacillus stearothermophilus neopullulanase. J Mol Biol 326: 177-188
    • (2003) J Mol Biol , vol.326 , pp. 177-188
    • Hondoh, H.1    Kuriki, T.2    Matsuura, Y.3
  • 27
    • 0037417869 scopus 로고    scopus 로고
    • Crystal structure of the MurG:UDP-GlcNAc complex reveals common structural principles of a superfamily of glycosyltransferases
    • Hu Y, Chen L, Ha S, Gross B, Falcone B, Walker D, Mokhtarzadeh M, Walker S (2003) Crystal structure of the MurG:UDP-GlcNAc complex reveals common structural principles of a superfamily of glycosyltransferases. Proc Natl Acad Sci USA 100: 845-849
    • (2003) Proc Natl Acad Sci USA , vol.100 , pp. 845-849
    • Hu, Y.1    Chen, L.2    Ha, S.3    Gross, B.4    Falcone, B.5    Walker, D.6    Mokhtarzadeh, M.7    Walker, S.8
  • 28
    • 0026562948 scopus 로고
    • Glycogen phosphorylase: Control by phosphorylation and allosteric effectors
    • Johnson LN (1992) Glycogen phosphorylase: control by phosphorylation and allosteric effectors. FASEB J 6: 2274-2282
    • (1992) FASEB J , vol.6 , pp. 2274-2282
    • Johnson, L.N.1
  • 29
    • 0025217008 scopus 로고
    • Refined crystal structure of the phosphorylase-heptulose 2-phos-phate-oligosaccharide-AMP complex
    • Johnson LN, Acharya KR, Jordan MD, McLaughlin PJ (1990) Refined crystal structure of the phosphorylase-heptulose 2-phos-phate-oligosaccharide-AMP complex. J Mol Biol 211: 645-661
    • (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
  • 30
    • 84889120137 scopus 로고
    • Improved methods for building protein models in electron density maps and the location of errors in these models
    • Jones TA, Zou JY, Cowan SW, Kjeldgaard M (1991) Improved methods for building protein models in electron density maps and the location of errors in these models. Acta Crystallogr D 47: 110-119
    • (1991) Acta Crystallogr D , vol.47 , pp. 110-119
    • Jones, T.A.1    Zou, J.Y.2    Cowan, S.W.3    Kjeldgaard, M.4
  • 31
  • 32
    • 0007486292 scopus 로고
    • Biosynthesis of glycogen from uridine diphosphate glucose
    • Leloir LF, Cardini CE (1957) Biosynthesis of glycogen from uridine diphosphate glucose. J Am Chem Soc 79: 6340-6341
    • (1957) J Am Chem Soc , vol.79 , pp. 6340-6341
    • Leloir, L.F.1    Cardini, C.E.2
  • 33
    • 0036328625 scopus 로고    scopus 로고
    • Possible structure and active site residues of starch, glycogen, and sucrose syntheses
    • MacGregor EA (2002) Possible structure and active site residues of starch, glycogen, and sucrose syntheses. J Prot Chem 21: 297-306
    • (2002) J Prot Chem , vol.21 , pp. 297-306
    • MacGregor, E.A.1
  • 34
    • 0023795303 scopus 로고
    • Catalytic site of rabbit glycogen synthase isozymes. Identification of an active site lysine close to the amino terminus of the subunit
    • Mahrenholz AM, Wang YH, Roach PJ (1988) Catalytic site of rabbit glycogen synthase isozymes. Identification of an active site lysine close to the amino terminus of the subunit. J Biol Chem 263: 10561-10567
    • (1988) J Biol Chem , vol.263 , pp. 10561-10567
    • Mahrenholz, A.M.1    Wang, Y.H.2    Roach, P.J.3
  • 35
    • 0029744440 scopus 로고    scopus 로고
    • Increased glycogen accumulation in transgenic mice overexpressing glycogen synthase in skeletal muscle
    • Manchester J, Skurat AV, Roach P, Hauschka SD, Lawrence JC (1996) Increased glycogen accumulation in transgenic mice overexpressing glycogen synthase in skeletal muscle. Proc Natl Acad Sci USA 93: 10707-10711
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 10707-10711
    • Manchester, J.1    Skurat, A.V.2    Roach, P.3    Hauschka, S.D.4    Lawrence, J.C.5
  • 36
    • 0035902864 scopus 로고    scopus 로고
    • High resolution crystal structures of T4 phage beta-glucosyltransferase: Induced fit and effect of substrate and metal binding
    • Morera S, Lariviere L, Kurzeck J, Aschke-Sonnenborn U, Freemont PS, Janin J, Ruger W (2001) High resolution crystal structures of T4 phage beta-glucosyltransferase: induced fit and effect of substrate and metal binding. J Mol Biol 311: 569-577
    • (2001) J Mol Biol , vol.311 , pp. 569-577
    • Morera, S.1    Lariviere, L.2    Kurzeck, J.3    Aschke-Sonnenborn, U.4    Freemont, P.S.5    Janin, J.6    Ruger, W.7
  • 37
    • 0034604255 scopus 로고    scopus 로고
    • Involvement of conserved aspartate and glutamate residues in the catalysis and substrate binding of maize starch synthase
    • Nichols DJ, Keeling PL, Spalding M, Guan H (2000) Involvement of conserved aspartate and glutamate residues in the catalysis and substrate binding of maize starch synthase. Biochemistry 39: 7820-7825
    • (2000) Biochemistry , vol.39 , pp. 7820-7825
    • Nichols, D.J.1    Keeling, P.L.2    Spalding, M.3    Guan, H.4
  • 38
    • 0034623162 scopus 로고    scopus 로고
    • Regulation of glycogen synthase. Identification of residues involved in regulation by the allosteric ligand glucose-6-P and by phosphorylation
    • Pederson BA, Cheng C, Wilson WA, Roach PJ (2000) Regulation of glycogen synthase. Identification of residues involved in regulation by the allosteric ligand glucose-6-P and by phosphorylation. J Biol Chem 275: 27753-27761
    • (2000) J Biol Chem , vol.275 , pp. 27753-27761
    • Pederson, B.A.1    Cheng, C.2    Wilson, W.A.3    Roach, P.J.4
  • 40
    • 0036079974 scopus 로고    scopus 로고
    • Glycogen and its metabolism
    • Roach PJ (2002) Glycogen and its metabolism. Curr Mol Med 2: 101-120
    • (2002) Curr Mol Med , vol.2 , pp. 101-120
    • Roach, P.J.1
  • 41
    • 0035936763 scopus 로고    scopus 로고
    • New perspectives into the molecular pathogenesis and treatment of type 2 diabetes
    • Saltiel AR (2001) New perspectives into the molecular pathogenesis and treatment of type 2 diabetes. Cell 104: 517-529
    • (2001) Cell , vol.104 , pp. 517-529
    • Saltiel, A.R.1
  • 42
    • 0029049719 scopus 로고
    • Phosphorylation of sites 3a and 3b (Ser640 and Ser644) in the control of rabbit muscle glycogen synthase
    • Skurat AV, Roach PJ (1995) Phosphorylation of sites 3a and 3b (Ser640 and Ser644) in the control of rabbit muscle glycogen synthase. J Biol Chem 270: 12491-12497
    • (1995) J Biol Chem , vol.270 , pp. 12491-12497
    • Skurat, A.V.1    Roach, P.J.2
  • 43
    • 0027968068 scopus 로고
    • CLUSTAL W: Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice
    • Thompson JD, Higgins DG, Gibson TJ (1994) CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice. Nucleic Acids Res 22: 4673-4680
    • (1994) Nucleic Acids Res , vol.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3
  • 44
    • 0141703314 scopus 로고    scopus 로고
    • De novo synthesis of bacterial glycogen: Agrobacterium tumefaciens glycogen synthase is involved in glucan initiation and elongation
    • Ugalde JE, Parodi AJ, Ugalde RA (2003) De novo synthesis of bacterial glycogen: Agrobacterium tumefaciens glycogen synthase is involved in glucan initiation and elongation. Proc Natl Acad Sci USA 100: 10659-10663
    • (2003) Proc Natl Acad Sci USA , vol.100 , pp. 10659-10663
    • Ugalde, J.E.1    Parodi, A.J.2    Ugalde, R.A.3
  • 45
    • 0027965664 scopus 로고
    • Crystal structure of the DNA modifying enzyme beta-glucosyltransferase in the presence and absence of the substrate uridine diphosphoglucose
    • Vrielink A, Ruger W, Driessen HP, Freemont PS (1994) Crystal structure of the DNA modifying enzyme beta-glucosyltransferase in the presence and absence of the substrate uridine diphosphoglucose. EMBO J 13: 3413-3422
    • (1994) EMBO J , vol.13 , pp. 3413-3422
    • Vrielink, A.1    Ruger, W.2    Driessen, H.P.3    Freemont, P.S.4
  • 46
    • 0031014875 scopus 로고    scopus 로고
    • The crystal structure of Escherichia coli maltodextrin phosphorylase provides an explanation for the activity without control in this basic archetype of a phosphorylase
    • Watson KA, Schinzel R, Palm D, Johnson LN (1997) The crystal structure of Escherichia coli maltodextrin phosphorylase provides an explanation for the activity without control in this basic archetype of a phosphorylase. EMBO J 16: 1-14
    • (1997) EMBO J , vol.16 , pp. 1-14
    • Watson, K.A.1    Schinzel, R.2    Palm, D.3    Johnson, L.N.4
  • 47
    • 0033082065 scopus 로고    scopus 로고
    • Optimizing Shake-and-Bake for proteins
    • Weeks CM, Miller R (1999) Optimizing Shake-and-Bake for proteins. Acta Crystallogr D 55: 492-500
    • (1999) Acta Crystallogr D , vol.55 , pp. 492-500
    • Weeks, C.M.1    Miller, R.2
  • 48
    • 0035976715 scopus 로고    scopus 로고
    • Homology between O-linked GlcNAc transferases and proteins of the glycogen phosphorylase superfamily
    • Wrabl JO, Grishin NV (2001) Homology between O-linked GlcNAc transferases and proteins of the glycogen phosphorylase superfamily. J Mol Biol 314: 365-374
    • (2001) J Mol Biol , vol.314 , pp. 365-374
    • Wrabl, J.O.1    Grishin, N.V.2
  • 49
    • 1542319703 scopus 로고    scopus 로고
    • Identification and characterization of a critical region in the glycogen synthase from Escherichia coli
    • Yep A, Ballicora MA, Sivak MN, Preiss J (2004) Identification and characterization of a critical region in the glycogen synthase from Escherichia coli. J Biol Chem 279: 8359-8367
    • (2004) J Biol Chem , vol.279 , pp. 8359-8367
    • Yep, A.1    Ballicora, M.A.2    Sivak, M.N.3    Preiss, J.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.