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PDBsum entry 7gpb
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Glycogen phosphorylase PDB id
7gpb

 

 

 

 

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JSmol PyMol  
Contents
Protein chains
824 a.a. *
Ligands
SO4 ×7
PLP ×4
AMP ×4
* Residue conservation analysis
PDB id:
7gpb
Name: Glycogen phosphorylase
Title: Structural mechanism for glycogen phosphorylase control by phosphorylation and amp
Structure: Glycogen phosphorylase b. Chain: a, b, c, d. Engineered: yes
Source: Oryctolagus cuniculus. Rabbit. Organism_taxid: 9986
Biol. unit: Tetramer (from PQS)
Resolution:
2.90Å     R-factor:   0.171    
Authors: D.Barford,S.-H.Hu,L.N.Johnson
Key ref: D.Barford et al. (1991). Structural mechanism for glycogen phosphorylase control by phosphorylation and AMP. J Mol Biol, 218, 233-260. PubMed id: 1900534
Date:
13-Nov-90     Release date:   15-Oct-92    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chains
Pfam   ArchSchema ?
P00489  (PYGM_RABIT) -  Glycogen phosphorylase, muscle form from Oryctolagus cuniculus
Seq:
Struc: 		 
Seq:
Struc: 		843 a.a.
824 a.a.*
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 1 residue position (black cross)

 Enzyme reactions 
   Enzyme class: E.C.2.4.1.1  - glycogen phosphorylase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]

      Pathway: 		Glycogen
      Reaction: [(1->4)-alpha-D-glucosyl](n) + phosphate = [(1->4)-alpha-D-glucosyl](n-1) + alpha-D-glucose 1-phosphate
[(1->4)-alpha-D-glucosyl](n)
 + phosphate
 = [(1->4)-alpha-D-glucosyl](n-1)
 +
alpha-D-glucose 1-phosphate
Bound ligand (Het Group name = AMP)
matches with 50.00% similarity
Molecule diagrams generated from .mol files obtained from the KEGG ftp site

 

 
    Added reference    
 
 
J Mol Biol 218:233-260 (1991)
PubMed id: 1900534  
 
 
Structural mechanism for glycogen phosphorylase control by phosphorylation and AMP.
D.Barford, S.H.Hu, L.N.Johnson.
 
  ABSTRACT  
 
The crystal structures of activated R state glycogen phosphorylase a (GPa) and R and T state glycogen phosphorylase b (GPb) complexed with AMP have been solved at 2.9 A, 2.9 A and 2.2 A resolution, respectively. The structure of R state GPa is nearly identical to the structure of sulphate-activated R state GPb, except in the region of Ser14, where there is a covalently attached phosphate group in GPa and a non-covalently attached sulphate group in GPb. The contacts made by the N-terminal tail residues in R state GPa at the subunit interface of the functionally active dimer are similar to those observed previously for T state GPa. The quaternary and tertiary structural changes on the T to R transition allow these interactions to be relayed to the catalytic site in R state GPa. The transition from the T state GPb structure to the R state GPa structure results in a change in the N-terminal residues from a poorly ordered extended structure that makes intrasubunit contacts to an ordered coiled conformation that makes intersubunit contacts. The distance between Arg10, the first residue to be located from the N terminus, in R state GPa and T state GPb is 50 A. One of the important subunit-subunit interactions in the dimer molecule involves contacts between the helix alpha 2 and the cap' (residues 35' to 45' that form a loop between the 1st and 2nd alpha helices, alpha 1' and alpha 2' of the other subunit. The prime denotes residues from the other subunit). The interactions made by the N-terminal residues induce structural changes at the cap'/alpha 2 helix interface that lead to the creation of a high-affinity AMP site. The tertiary structural changes at the cap (shifts 1.2 to 2.1 A for residues 35 to 45) are partially compensated by the quaternary structural change so that the overall shifts in these residues after the combined tertiary and quaternary changes are between 0.5 and 1.3 A. AMP binds to R state GPb with at least 100-fold greater affinity and exhibits four additional hydrogen bonds, stronger ionic interactions and more extensive van der Waals' interactions with 116 A2 greater solvent accessible surface area buried compared with AMP bound to T state GPb.(ABSTRACT TRUNCATED AT 400 WORDS)
 

Literature references that cite this PDB file's key reference

  PubMed id Reference
23211768 D.Barford, and D.I.Stuart (2012).
Louise N. Johnson 1940-2012.
  Nat Struct Mol Biol, 19, 1216-1217.  
21035757 M.Bouskila, R.W.Hunter, A.F.Ibrahim, L.Delattre, M.Peggie, J.A.van Diepen, P.J.Voshol, J.Jensen, and K.Sakamoto (2010).
Allosteric regulation of glycogen synthase controls glycogen synthesis in muscle.
  Cell Metab, 12, 456-466.  
20409458 X.Liu, L.Bardwell, and Q.Nie (2010).
A combination of multisite phosphorylation and substrate sequestration produces switchlike responses.
  Biophys J, 98, 1396-1407.  
18198182 A.Pautsch, N.Stadler, O.Wissdorf, E.Langkopf, W.Moreth, and R.Streicher (2008).
Molecular recognition of the protein phosphatase 1 glycogen targeting subunit by glycogen phosphorylase.
  J Biol Chem, 283, 8913-8918.
PDB code: 2qll
17957766 M.D.Daily, T.J.Upadhyaya, and J.J.Gray (2008).
Contact rearrangements form coupled networks from local motions in allosteric proteins.
  Proteins, 71, 455-466.  
17600143 C.Tiraidis, K.M.Alexacou, S.E.Zographos, D.D.Leonidas, T.Gimisis, and N.G.Oikonomakos (2007).
FR258900, a potential anti-hyperglycemic drug, binds at the allosteric site of glycogen phosphorylase.
  Protein Sci, 16, 1773-1782.
PDB code: 2off
18075577 J.Kuriyan, and D.Eisenberg (2007).
The origin of protein interactions and allostery in colocalization.
  Nature, 450, 983-990.  
17521420 J.L.Jiménez, B.Hegemann, J.R.Hutchins, J.M.Peters, and R.Durbin (2007).
A systematic comparative and structural analysis of protein phosphorylation sites based on the mtcPTM database.
  Genome Biol, 8, R90.  
17295319 M.D.Daily, and J.J.Gray (2007).
Local motions in a benchmark of allosteric proteins.
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17289565 Z.Serber, and J.E.Ferrell (2007).
Tuning bulk electrostatics to regulate protein function.
  Cell, 128, 441-444.  
16691548 C.Cuadri-Tomé, C.Barón, V.Jara-Pérez, A.Parody-Morreale, J.C.Martinez, and A.Cámara-Artigas (2006).
Kinetic analysis and modelling of the allosteric behaviour of liver and muscle glycogen phosphorylases.
  J Mol Recognit, 19, 451-457.  
16523484 C.M.Lukacs, N.G.Oikonomakos, R.L.Crowther, L.N.Hong, R.U.Kammlott, W.Levin, S.Li, C.M.Liu, D.Lucas-McGady, S.Pietranico, and L.Reik (2006).
The crystal structure of human muscle glycogen phosphorylase a with bound glucose and AMP: an intermediate conformation with T-state and R-state features.
  Proteins, 63, 1123-1126.
PDB code: 1z8d
16371327 F.Magkos, and S.A.Kavouras (2005).
Caffeine use in sports, pharmacokinetics in man, and cellular mechanisms of action.
  Crit Rev Food Sci Nutr, 45, 535-562.  
15987904 N.G.Oikonomakos, M.N.Kosmopoulou, E.D.Chrysina, D.D.Leonidas, I.D.Kostas, K.U.Wendt, T.Klabunde, and E.Defossa (2005).
Crystallographic studies on acyl ureas, a new class of glycogen phosphorylase inhibitors, as potential antidiabetic drugs.
  Protein Sci, 14, 1760-1771.
PDB codes: 1wut 1wuy 1wv0 1wv1
14563176 G.Wu, and M.Müller (2003).
Glycogen phosphorylase sequences from the amitochondriate protists, Trichomonas vaginalis, Mastigamoeba balamuthi, Entamoeba histolytica and Giardia intestinalis.
  J Eukaryot Microbiol, 50, 366-372.  
11796108 C.Vénien-Bryan, E.M.Lowe, N.Boisset, K.W.Traxler, L.N.Johnson, and G.M.Carlson (2002).
Three-dimensional structure of phosphorylase kinase at 22 A resolution and its complex with glycogen phosphorylase b.
  Structure, 10, 33-41.  
12025402 H.Kojima, and O.Numata (2002).
Enzymatic form and cytoskeletal form of bifunctional Tetrahymena 49kDa protein is regulated by phosphorylation.
  Zoolog Sci, 19, 37-42.  
11895439 N.G.Oikonomakos, M.Kosmopoulou, S.E.Zographos, D.D.Leonidas, E.D.Chrysina, L.Somsák, V.Nagy, J.P.Praly, T.Docsa, B.Tóth, and P.Gergely (2002).
Binding of N-acetyl-N '-beta-D-glucopyranosyl urea and N-benzoyl-N '-beta-D-glucopyranosyl urea to glycogen phosphorylase b: kinetic and crystallographic studies.
  Eur J Biochem, 269, 1684-1696.
PDB codes: 1k06 1k08 1k0q 1kti
11340058 J.L.Buchbinder, V.L.Rath, and R.J.Fletterick (2001).
Structural relationships among regulated and unregulated phosphorylases.
  Annu Rev Biophys Biomol Struct, 30, 191-209.  
11168388 N.A.Chebotareva, S.E.Harding, and D.J.Winzor (2001).
Ultracentrifugal studies of the effect of molecular crowding by trimethylamine N-oxide on the self-association of muscle glycogen phosphorylase b.
  Eur J Biochem, 268, 506-513.  
11488924 S.W.Vetter, and E.Leclerc (2001).
Phosphorylation of serine residues affects the conformation of the calmodulin binding domain of human protein 4.1.
  Eur J Biochem, 268, 4292-4299.  
11123915 A.C.Biorn, C.Bartleson, and D.J.Graves (2000).
Site-directed mutants of glycogen phosphorylase are altered in their interaction with phosphorylase kinase.
  Biochemistry, 39, 15887-15894.  
11304673 I.Hamachi, J.I.Watanabe, R.Eboshi, T.Hiraoka, and S.Shinkai (2000).
Incorporation of artificial receptors into a protein/peptide surface: a strategy for on/off type of switching of semisynthetic enzymes.
  Biopolymers, 55, 459-468.  
10873856 N.G.Oikonomakos, V.T.Skamnaki, K.E.Tsitsanou, N.G.Gavalas, and L.N.Johnson (2000).
A new allosteric site in glycogen phosphorylase b as a target for drug interactions.
  Structure, 8, 575-584.
PDB code: 1c50
  10892808 R.Griessler, S.D'Auria, F.Tanfani, and B.Nidetzky (2000).
Thermal denaturation pathway of starch phosphorylase from Corynebacterium callunae: oxyanion binding provides the glue that efficiently stabilizes the dimer structure of the protein.
  Protein Sci, 9, 1149-1161.  
10545187 A.A.Komissarov, and S.L.Deutscher (1999).
Thermodynamics of Fab-ssDNA interactions: contribution of heavy chain complementarity determining region 3.
  Biochemistry, 38, 14631-14637.  
9876124 A.Tholey, A.Lindemann, V.Kinzel, and J.Reed (1999).
Direct effects of phosphorylation on the preferred backbone conformation of peptides: a nuclear magnetic resonance study.
  Biophys J, 76, 76-87.  
10454193 D.Graves, C.Bartleson, A.Biorn, and M.Pete (1999).
Substrate and inhibitor recognition of protein kinases: what is known about the catalytic subunit of phosphorylase kinase?
  Pharmacol Ther, 82, 143-155.  
10563798 G.Kung, J.A.Runquist, H.M.Miziorko, and D.H.Harrison (1999).
Identification of the allosteric regulatory site in bacterial phosphoribulokinase.
  Biochemistry, 38, 15157-15165.  
10223296 K.A.Denessiouk, A.I.Denesyuk, J.V.Lehtonen, T.Korpela, and M.S.Johnson (1999).
Common structural elements in the architecture of the cofactor-binding domains in unrelated families of pyridoxal phosphate-dependent enzymes.
  Proteins, 35, 250-261.  
10469642 K.A.Watson, C.McCleverty, S.Geremia, S.Cottaz, H.Driguez, and L.N.Johnson (1999).
Phosphorylase recognition and phosphorolysis of its oligosaccharide substrate: answers to a long outstanding question.
  EMBO J, 18, 4619-4632.
PDB codes: 1e4o 1qm5
  10211820 K.E.Tsitsanou, N.G.Oikonomakos, S.E.Zographos, V.T.Skamnaki, M.Gregoriou, K.A.Watson, L.N.Johnson, and G.W.Fleet (1999).
Effects of commonly used cryoprotectants on glycogen phosphorylase activity and structure.
  Protein Sci, 8, 741-749.
PDB codes: 1b4d 1bx3
  10548038 N.G.Oikonomakos, K.E.Tsitsanou, S.E.Zographos, V.T.Skamnaki, S.Goldmann, and H.Bischoff (1999).
Allosteric inhibition of glycogen phosphorylase a by the potential antidiabetic drug 3-isopropyl 4-(2-chlorophenyl)-1,4-dihydro-1-ethyl-2-methyl-pyridine-3,5,6-tricarbo xylate.
  Protein Sci, 8, 1930-1945.
PDB codes: 2gpa 3amv
10092844 Z.X.Wang (1999).
Kinetic study on the dimer-tetramer interconversion of glycogen phosphorylase a.
  Eur J Biochem, 259, 609-617.  
9632643 A.Pappas, W.L.Yang, T.S.Park, and G.M.Carman (1998).
Nucleotide-dependent tetramerization of CTP synthetase from Saccharomyces cerevisiae.
  J Biol Chem, 273, 15954-15960.  
  9568898 M.Gregoriou, M.E.Noble, K.A.Watson, E.F.Garman, T.M.Krulle, C.de la Fuente, G.W.Fleet, N.G.Oikonomakos, and L.N.Johnson (1998).
The structure of a glycogen phosphorylase glucopyranose spirohydantoin complex at 1.8 A resolution and 100 K: the role of the water structure and its contribution to binding.
  Protein Sci, 7, 915-927.
PDB codes: 1a8i 2gpn
9548941 M.Schutkowski, A.Bernhardt, X.Z.Zhou, M.Shen, U.Reimer, J.U.Rahfeld, K.P.Lu, and G.Fischer (1998).
Role of phosphorylation in determining the backbone dynamics of the serine/threonine-proline motif and Pin1 substrate recognition.
  Biochemistry, 37, 5566-5575.  
9251252 A.Cámara-Artigas, A.Parody-Morreale, and C.Barón (1997).
Analogous activation of bovine liver glycogen phosphorylase by AMP and IMP.
  Int J Biochem Cell Biol, 29, 849-856.  
9218476 A.Nilsson, D.Stys, T.Drakenberg, M.D.Spangfort, S.Forsén, and J.F.Allen (1997).
Phosphorylation controls the three-dimensional structure of plant light harvesting complex II.
  J Biol Chem, 272, 18350-18357.  
  9194198 B.Kobe, I.G.Jennings, C.M.House, S.C.Feil, B.J.Michell, T.Tiganis, M.W.Parker, R.G.Cotton, and B.E.Kemp (1997).
Regulation and crystallization of phosphorylated and dephosphorylated forms of truncated dimeric phenylalanine hydroxylase.
  Protein Sci, 6, 1352-1357.  
9208914 D.G.Hardie, and D.Carling (1997).
The AMP-activated protein kinase--fuel gauge of the mammalian cell?
  Eur J Biochem, 246, 259-273.  
9362479 E.D.Lowe, M.E.Noble, V.T.Skamnaki, N.G.Oikonomakos, D.J.Owen, and L.N.Johnson (1997).
The crystal structure of a phosphorylase kinase peptide substrate complex: kinase substrate recognition.
  EMBO J, 16, 6646-6658.
PDB code: 2phk
9201951 J.L.Buchbinder, C.B.Luong, M.F.Browner, and R.J.Fletterick (1997).
Partial activation of muscle phosphorylase by replacement of serine 14 with acidic residues at the site of regulatory phosphorylation.
  Biochemistry, 36, 8039-8044.  
9009262 K.A.Watson, R.Schinzel, D.Palm, and L.N.Johnson (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.  
9384566 K.Lin, P.K.Hwang, and R.J.Fletterick (1997).
Distinct phosphorylation signals converge at the catalytic center in glycogen phosphorylases.
  Structure, 5, 1511-1523.  
9341222 M.Chandra, W.J.Dong, B.S.Pan, H.C.Cheung, and R.J.Solaro (1997).
Effects of protein kinase A phosphorylation on signaling between cardiac troponin I and the N-terminal domain of cardiac troponin C.
  Biochemistry, 36, 13305-13311.  
9145112 M.O'Reilly, K.A.Watson, R.Schinzel, D.Palm, and L.N.Johnson (1997).
Oligosaccharide substrate binding in Escherichia coli maltodextrin phosphorylase.
  Nat Struct Biol, 4, 405-412.
PDB code: 1ahp
9384557 S.E.Zographos, N.G.Oikonomakos, K.E.Tsitsanou, D.D.Leonidas, E.D.Chrysina, V.T.Skamnaki, H.Bischoff, S.Goldmann, K.A.Watson, and L.N.Johnson (1997).
The structure of glycogen phosphorylase b with an alkyldihydropyridine-dicarboxylic acid compound, a novel and potent inhibitor.
  Structure, 5, 1413-1425.
PDB codes: 1amv 2amv
8994875 D.E.Koshland (1996).
The structural basis of negative cooperativity: receptors and enzymes.
  Curr Opin Struct Biol, 6, 757-761.  
8652510 E.P.Mitchell, S.G.Withers, P.Ermert, A.T.Vasella, E.F.Garman, N.G.Oikonomakos, and L.N.Johnson (1996).
Ternary complex crystal structures of glycogen phosphorylase with the transition state analogue nojirimycin tetrazole and phosphate in the T and R states.
  Biochemistry, 35, 7341-7355.
PDB codes: 1noi 1noj 1nok
8798388 J.L.Buchbinder, and R.J.Fletterick (1996).
Role of the active site gate of glycogen phosphorylase in allosteric inhibition and substrate binding.
  J Biol Chem, 271, 22305-22309.  
9000033 J.Stubbe, and L.N.Johnson (1996).
Catalysis and regulation.
  Curr Opin Struct Biol, 6, 733-735.  
8910343 L.García-Fuentes, A.Cámara-Artigas, O.López-Mayorga, and C.Barón (1996).
Thermodynamic characterization of 5'-AMP binding to bovine liver glycogen phosphorylase a.
  J Biol Chem, 271, 27569-27574.  
8994876 L.N.Johnson, and M.O'Reilly (1996).
Control by phosphorylation.
  Curr Opin Struct Biol, 6, 762-769.  
  8976550 N.G.Oikonomakos, S.E.Zographos, K.E.Tsitsanou, L.N.Johnson, and K.R.Acharya (1996).
Activator anion binding site in pyridoxal phosphorylase b: the binding of phosphite, phosphate, and fluorophosphate in the crystal.
  Protein Sci, 5, 2416-2428.
PDB codes: 1skc 1skd 1ske 2skc 2skd 2ske
8780518 R.Croce, J.Breton, and R.Bassi (1996).
Conformational changes induced by phosphorylation in the CP29 subunit of photosystem II.
  Biochemistry, 35, 11142-11148.  
8702602 R.T.Pickard, X.G.Chiou, B.A.Strifler, M.R.DeFelippis, P.A.Hyslop, A.L.Tebbe, Y.K.Yee, L.J.Reynolds, E.A.Dennis, R.M.Kramer, and J.D.Sharp (1996).
Identification of essential residues for the catalytic function of 85-kDa cytosolic phospholipase A2. Probing the role of histidine, aspartic acid, cysteine, and arginine.
  J Biol Chem, 271, 19225-19231.  
8740368 V.L.Rath, K.Lin, P.K.Hwang, and R.J.Fletterick (1996).
The evolution of an allosteric site in phosphorylase.
  Structure, 4, 463-473.  
8942672 W.G.Stirtan, and S.G.Withers (1996).
Phosphonate and alpha-fluorophosphonate analogue probes of the ionization state of pyridoxal 5'-phosphate (PLP) in glycogen phosphorylase.
  Biochemistry, 35, 15057-15064.  
7744850 A.Cuenda, M.Nogues, F.Henao, and C.Gutiérrez-Merino (1995).
Interaction between glycogen phosphorylase and sarcoplasmic reticulum membranes and its functional implications.
  J Biol Chem, 270, 11998-12004.  
7579652 D.J.Matthews (1995).
Interfacial metal-binding site design.
  Curr Opin Biotechnol, 6, 419-424.  
7584626 F.San Juan Serrano, J.L.Sánchez López, and L.O.García Martín (1995).
Caffeine inhibition of glycogen phosphorylase from Mytilus galloprovincialis mantle tissue.
  Int J Biochem Cell Biol, 27, 911-916.  
7584627 F.San Juan Serrano, M.Fernández González, J.L.Sánchez López, and L.O.García Martín (1995).
Modification of kinetic parameters of glycogen phosphorylase from mantle tissue of Mytilus galloprovincialis by a phosphorylation mechanism.
  Int J Biochem Cell Biol, 27, 917-922.  
7737174 M.Board, M.Hadwen, and L.N.Johnson (1995).
Effects of novel analogues of D-glucose on glycogen phosphorylase activities in crude extracts of liver and skeletal muscle.
  Eur J Biochem, 228, 753-761.  
7775430 M.M.Crerar, O.Karlsson, R.J.Fletterick, and P.K.Hwang (1995).
Chimeric muscle and brain glycogen phosphorylases define protein domains governing isozyme-specific responses to allosteric activation.
  J Biol Chem, 270, 13748-13756.  
  8580837 N.G.Oikonomakos, M.Kontou, S.E.Zographos, K.A.Watson, L.N.Johnson, C.J.Bichard, G.W.Fleet, and K.R.Acharya (1995).
N-acetyl-beta-D-glucopyranosylamine: a potent T-state inhibitor of glycogen phosphorylase. A comparison with alpha-D-glucose.
  Protein Sci, 4, 2469-2477.
PDB codes: 1prj 2prj
  7987213 E.M.Duke, S.Wakatsuki, A.Hadfield, and L.N.Johnson (1994).
Laue and monochromatic diffraction studies on catalysis in phosphorylase b crystals.
  Protein Sci, 3, 1178-1196.  
  7849589 L.N.Johnson, and D.Barford (1994).
Electrostatic effects in the control of glycogen phosphorylase by phosphorylation.
  Protein Sci, 3, 1726-1730.  
7922041 Y.Harpaz, M.Gerstein, and C.Chothia (1994).
Volume changes on protein folding.
  Structure, 2, 641-649.  
8457673 J.E.Taguchi, S.J.Heyes, D.Barford, L.N.Johnson, and C.M.Dobson (1993).
Solid state 31P cross-polarization/magic angle sample spinning nuclear magnetic resonance of crystalline glycogen phosphorylase b.
  Biophys J, 64, 492-501.  
  8336738 M.J.Marcote, D.R.Knighton, G.Basi, J.M.Sowadski, P.Brambilla, G.Draetta, and S.S.Taylor (1993).
A three-dimensional model of the Cdc2 protein kinase: localization of cyclin- and Suc1-binding regions and phosphorylation sites.
  Mol Cell Biol, 13, 5122-5131.  
  1304350 D.Barford, and L.N.Johnson (1992).
The molecular mechanism for the tetrameric association of glycogen phosphorylase promoted by protein phosphorylation.
  Protein Sci, 1, 472-493.  
  1304390 D.D.Leonidas, N.G.Oikonomakos, A.C.Papageorgiou, K.R.Acharya, D.Barford, and L.N.Johnson (1992).
Control of phosphorylase b conformation by a modified cofactor: crystallographic studies on R-state glycogen phosphorylase reconstituted with pyridoxal 5'-diphosphate.
  Protein Sci, 1, 1112-1122.
PDB code: 1abb
  1304391 D.D.Leonidas, N.G.Oikonomakos, A.C.Papageorgiou, and T.G.Sotiroudis (1992).
Kinetic properties of tetrameric glycogen phosphorylase b in solution and in the crystalline state.
  Protein Sci, 1, 1123-1132.  
1585448 J.F.Allen (1992).
How does protein phosphorylation regulate photosynthesis?
  Trends Biochem Sci, 17, 12-17.  
1566331 M.F.Browner, and R.J.Fletterick (1992).
Phosphorylase: a biological transducer.
  Trends Biochem Sci, 17, 66-71.  
1499569 S.M.Shaw, and E.A.Carrey (1992).
Regulation of the mammalian carbamoyl-phosphate synthetase II by effectors and phosphorylation. Altered affinity for ATP and magnesium ions measured using the ammonia-dependent part reaction.
  Eur J Biochem, 207, 957-965.  
  1304389 S.R.Sprang, N.B.Madsen, and S.G.Withers (1992).
Multiple phosphate positions in the catalytic site of glycogen phosphorylase: structure of the pyridoxal-5'-pyrophosphate coenzyme-substrate analog.
  Protein Sci, 1, 1100-1111.  
15336195 L.N.Johnson (1991).
Direct interaction or remote control?
  Curr Biol, 1, 17-19.  
The most recent references are shown first. Citation data come partly from CiteXplore and partly from an automated harvesting procedure. Note that this is likely to be only a partial list as not all journals are covered by either method. However, we are continually building up the citation data so more and more references will be included with time. Where a reference describes a PDB structure, the PDB code is shown on the right.

 

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