Role of side-chains in the operation of the main molecular hinge of 3-phosphoglycerate kinase

FEBS Letters

Volumn 582, Issue 9, 2008, Pages 1335-1340

  Szabó, Judit ^a   Varga, Andrea ^a   Flachner, Beáta ^a   Konarev, Peter V ^b,c   Svergun, Dmitri I ^b,c   Závodszky, Péter ^a   Vas, Mária ^a  

^a INSTITUTE OF EXPERIMENTAL MEDICINE   (Hungary)

^b DESY   (Germany)

^c SHUBNIKOV INSTITUTE OF CRYSTALLOGRAPHY   (Russian Federation)

Author keywords

3 Phosphoglycerate kinase; Domain movement; Hinge; Site directed mutagenesis; Small angle X ray scattering

Indexed keywords

PHOSPHOGLYCERATE KINASE;

ARTICLE; CATALYSIS; ENZYME ACTIVITY; ENZYME STRUCTURE; GENE DELETION; GENE MUTATION; PRIORITY JOURNAL;

CALORIMETRY, DIFFERENTIAL SCANNING; CIRCULAR DICHROISM; KINETICS; MODELS, MOLECULAR; MUTAGENESIS, SITE-DIRECTED; PHOSPHOGLYCERATE KINASE; PROTEIN CONFORMATION;

EID: 41449091478     PISSN: 00145793     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.febslet.2008.03.016     Document Type: Article

References (20)

1. Bahar I., Chennubhotla C., and Tobi D. Intrinsic dynamics of enzymes in the unbound state and relation to allosteric regulation. Curr. Opin. Struct. Biol. 17 (2007) 633-640
2. Henzler-Wildman K.A., Lei M., Thai V., Kerns S.J., Karplus M., and Kern D. A hierarchy of timescales in protein dynamics is linked to enzyme catalysis. Nature 450 (2007) 913-916
3. Harlos K., Vas M., and Blake C.C.F. Crystal structure of the binary complex of pig muscle phosphoglycerate kinase and its substrate 3-phospho-d-glycerate. Proteins 12 (1992) 133-144
4. Flachner B., Kovári Z., Varga A., Gugolya Z., Vonderviszt F., Náray-Szabó G., and Vas M. Role of phosphate chain mobility of MgATP in completing the 3-phosphoglycerate kinase catalytic site: binding, kinetic, and crystallographic studies with ATP and MgATP. Biochemistry 43 (2004) 3436-3449
5. Davies G.J., Gamblin S.J., Littlechild J.A., Dauter Z., Wilson K.S., and Watson H.C. Structure of the ADP complex of the 3-phosphoglycerate kinase from Bacillus stearothermophilus at 1.65 A. Acta Crystallogr. D 50 (1994) 202-209
6. Szilágyi A.N., Ghosh M., Garman E., and Vas M. A 1.8 A resolution structure of pig muscle 3-phosphoglycerate kinase with bound MgADP and 3-phosphoglycerate in open conformation: new insight into the role of the nucleotide in domain closure. J. Mol. Biol. 306 (2001) 499-511
7. Varga A., Flachner B., Konarev P., Gráczer E., Szabó J., Svergun D., Závodszky P., and Vas M. Substrate-induced double sided H-bond network as a means of domain closure in 3-phosphoglycerate kinase. FEBS Lett. 580 (2006) 2698-2706
8. Mas M.T., Bailey J.M., and Resplandor Z.E. Site-directed mutagenesis of histidine-388 in the hinge region of yeast 3-phosphoglycerate kinase: effects on catalytic activity and activation by sulfate. Biochemistry 27 (1988) 1168-1172
9. Joao H.C., Taddei N., and Williams R.J. Investigating interdomain region mutants Phe194- - - -Leu and Phe194- - - -Trp of yeast phosphoglycerate kinase by 1H-NMR spectroscopy. Eur. J. Biochem. 205 (1992) 93-104
10. Flachner B., Varga A., Szabó J., Barna L., Hajdú I., Gyimesi G., Závodszky P., and Vas M. Substrate-assisted movement of the catalytic Lys 215 during domain closure: site-directed mutagenesis studies of human 3-phosphoglycerate kinase. Biochemistry 44 (2005) 16853-16865
11. Furfine C.S., and Velick S.F. The acyl-enzyme intermediate and the kinetic mechanism of the glyceraldehyde 3-phosphate dehydrogenase reaction. J. Biol. Chem. 240 (1965) 844-855
12. Szilágyi A.N., and Vas M. Anion activation of 3-phosphoglycerate kinase requires domain closure. Biochemistry 37 (1998) 8551-8563
13. Cserpán I., and Vas M. Effects of substrates on the heat stability and on the reactivities of thiol groups of 3-phosphoglycerate kinase. Eur. J. Biochem. 131 (1983) 157-162
14. Roessle M.W., et al. Upgrade of the small-angle X-ray scattering beamline X33 at the European Molecular Biology Laboratory, Hamburg. J. Appl. Crystallogr. 40 (2007) s190-s194
15. Konarev P.V., Volkov V.V., Petoukhov M.V., and Svergun D.I. ATSAS 2.1, a program package for small-angle scattering data analysis. J. Appl. Crystallogr. 39 (2006) 277-286
16. Svergun D.I., Barberato C., and Koch M.H.J. CRYSOL - a program to evaluate X-ray solution scattering of biological macromolecules from atomic coordinates. J. Appl. Crystallogr. 28 (1995) 768-773
17. Bernstein B.E., and Hol W.G. Crystal structures of substrates and products bound to the phosphoglycerate kinase active site reveal the catalytic mechanism. Biochemistry 37 (1998) 4429-4436
18. Auerbach G., Huber R., Grättinger M., Zaiss K., Schurig H., Jaenicke R., and Jacob U. Closed structure of phosphoglycerate kinase from Thermotoga maritima reveals the catalytic mechanism and determinants of thermal stability. Structure 5 (1997) 1475-1483
19. Hayward S. Identification of specific interactions that drive ligand-induced closure in five enzymes with classic domain movements. J. Mol. Biol. 339 (2004) 1001-1021
20. Balog E., Laberge M., and Fidy J. The influence of interdomain interactions on the intradomain motions in yeast phosphoglycerate kinase: a molecular dynamics study. Biophys. J. 92 (2007) 1709-1716