Mutagenesis of the Dimer Interface Region of Corynebacterium callunae Starch Phosphorylase Perturbs the Phosphate-Dependent Conformational Relay that Enhances Oligomeric Stability of the Enzyme

Journal of Biochemistry

Volumn 134, Issue 4, 2003, Pages 599-606

  Nidetzky, Bernd ^a   Griessler, Richard ^a   Pierfederici, Francesco Maria ^a,c   Psik, Barbara ^a   Sciré, Andrea ^b   Tanfani, Fabio ^b  

^a GRAZ UNIVERSITY OF TECHNOLOGY   (Austria)

^b UNIVERSITÀ POLITECNICA DELLE MARCHE   (Italy)

^c UNIVERSITY OF CATANIA   (Italy)

Author keywords

Dimer interface; FT IR spectroscopy; Long range interactions; Oligomeric structure; Starch phosphorylase

Indexed keywords

AMIDE; ANION; MUTANT PROTEIN; PHOSPHATE; STARCH PHOSPHORYLASE;

ARTICLE; BINDING AFFINITY; CORRELATION ANALYSIS; CORYNEBACTERIUM; ENZYME ACTIVITY; ENZYME CONFORMATION; ENZYME DENATURATION; ENZYME PURIFICATION; ENZYME STABILITY; HEATING; INFRARED SPECTROSCOPY; OLIGOMERIZATION; PROTEIN BINDING; PROTEIN QUATERNARY STRUCTURE; PROTEIN STRUCTURE; ROOM TEMPERATURE; SITE DIRECTED MUTAGENESIS; STRUCTURE ANALYSIS; WILD TYPE;

ALANINE; AMINO ACID SEQUENCE; CORYNEBACTERIUM; DIMERIZATION; HYDROGEN PEROXIDE; KINETICS; MOLECULAR SEQUENCE DATA; MUTAGENESIS, SITE-DIRECTED; MUTATION; PHOSPHATES; PLASMIDS; PROTEIN CONFORMATION; PROTEIN DENATURATION; PROTEIN STRUCTURE, QUATERNARY; SPECTROPHOTOMETRY, INFRARED; SPECTROSCOPY, FOURIER TRANSFORM INFRARED; STARCH PHOSPHORYLASE; TEMPERATURE;

CORYNEBACTERIUM; CORYNEBACTERIUM CALLUNAE; PROKARYOTA;

EID: 0344441359     PISSN: 0021924X     EISSN: None     Source Type: Journal    
DOI: 10.1093/jb/mvg178     Document Type: Article

References (15)

1. Mizoue, L.S. and Chazin, W.J. (2002) Engineering and design of ligand-induced conformational changes in proteins. Curr. Opin. Struct. Biol. 12, 459-463
2. Ahmad, A., Akhtar, M.S., and Bhakuni V. (2001) Monovalent cation-induced conformational change in glucose oxidase leading to stabilization of the enzyme. Biochemistry 40, 1945-1955
3. Griessler, R., D'Auria, S., Tanfani, F., and Nidetzky, B. (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
4. Griessler, R., Pickl M., D'Auria, S., Tanfani, F., and Nidetzky, B. (2001) Oxyanion-mediated protein stabilization: differential roles of phosphate for preventing inactivation of bacterial α-glucan phosphorylases. Biocat. Biotrans. 19, 379-398
5. Griessler, R., Schwarz, A., Mucha, J., and Nidetzky, B. (2003) Tracking interactions that stabilize the dimer structure of starch phosphorylase from Corynebacterium callunae: roles of Arg-234 and Arg-242 revealed by sequence analysis and site-directed mutagenesis. Eur. J. Biochem. 270, 2126-2136
6. Newgard, C.B., Hwang, P.K., and Fletterick, R.J. (1989) The family of glycogen phosphorylases: structure and function. Crit. Rev. Biochem. Mol. Biol. 24, 69-99
7. Weinhäusel, A., Griessler, R., Krebs, A., Zipper, P., Haltrich, D., Kulbe, K.D., and Nidetzky, B. (1997) α-1, 4-D-Glucan phosphorylase of gram-positive Corynebacterium callunae: isolation, biochemical properties and molecular shape of the enzyme from solution X-ray scattering. Biochem. J. 326, 773-783
8. Watson, K.A., Schinzel, R., Palm, D., and Johnson, L.N. (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
9. Johnson, L.N. (1992) Glycogen phosphorylase: control by phosphorylation and allosteric effectors. FASEB J. 6, 2274-2282
10. Buchbinder, J.L., Rath, V.L., and Fletterick, R.J. (2001) Structural relationships among regulated and unregulated phosphorylases. Annu. Rev. Biophys. Biomol. Struct. 30, 191-209
11. Copley, R.R. and Barton, G.J. (1994) A structural analysis of phosphate and sulfate binding sites in proteins. Estimation of propensities for binding and conservation of phosphate binding sites. J. Mol. Biol. 242, 321-329
12. Skorko-Glonek, J., Lipinska, B., Krzewski, K., Zolese, G., Bertoli, E., and Tanfani, F. (1997) HtrA heat-shock protease interacts with phospholipid membranes and undergoes conformational changes. J. Biol. Chem. 272, 8974-8982
13. Tanfani, F., Galeazzi, T., Curatola, G., Bertoli, E., and Ferretti, G. (1997) Reduced β-strand content in apoprotein B-100 in smaller and denser low-density lipoprotein subclasses as probed by Fourier-transform infrared spectroscopy. Biochem. J. 322, 765-769
14. Mäntele, M. (1993) Reaction-induced infrared difference spectroscopy for the study of protein function and reaction mechanisms. Trends Biochem. Sci. 18, 197-202
15. Meersman, F., Smeller, L., and Heremans, K. (2002) Comparative Fourier transform infrared spectroscopy study of cold-, pressure-, and heat-induced unfolding and aggregation of myoglobin. Biophys. J. 82, 2635-2644