메뉴 건너뛰기




Volumn 47, Issue 1, 2008, Pages 84-91

Infrared studies reveal unique vibrations associated with the PGK-ATP-3-PG ternary complex

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINETRIPHOSPHATE; BIOASSAY; CONFORMATIONS; INFRARED SPECTROSCOPY; NUCLEOTIDES;

EID: 37849049319     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi701723c     Document Type: Article
Times cited : (6)

References (36)
  • 3
    • 0035936656 scopus 로고    scopus 로고
    • 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
    • Szilagyi, A. N., Ghosh, M., Garman, E., and Vas, M. (2001) 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, 499-511.
    • (2001) J. Mol. Biol , vol.306 , pp. 499-511
    • Szilagyi, A.N.1    Ghosh, M.2    Garman, E.3    Vas, M.4
  • 4
    • 17444381136 scopus 로고    scopus 로고
    • Correlation between conformational stability of the ternary enzyme-substrate complex and domain closure of 3-phosphoglycerate kinase
    • Varga, A., Flachner, B., Graczer, E., Osvath, S., Szilagyi, A. N., and Vas, M. (2005) Correlation between conformational stability of the ternary enzyme-substrate complex and domain closure of 3-phosphoglycerate kinase, FEBS J. 272, 1867-1885.
    • (2005) FEBS J , vol.272 , pp. 1867-1885
    • Varga, A.1    Flachner, B.2    Graczer, E.3    Osvath, S.4    Szilagyi, A.N.5    Vas, M.6
  • 5
    • 33646174431 scopus 로고    scopus 로고
    • Substrate-induced double sided H-bond network as a means of domain closure in 3-phosphoglycerate kinase
    • Varga, A., Flachner, B., Konarev, P., Graczer, E., Szabo, J., Svergun, D., Zavodszky, P., and Vas, M. (2006) Substrate-induced double sided H-bond network as a means of domain closure in 3-phosphoglycerate kinase, FEBS Lett. 580, 2698-2706.
    • (2006) FEBS Lett , vol.580 , pp. 2698-2706
    • Varga, A.1    Flachner, B.2    Konarev, P.3    Graczer, E.4    Szabo, J.5    Svergun, D.6    Zavodszky, P.7    Vas, M.8
  • 6
    • 0031573453 scopus 로고    scopus 로고
    • Closed structure of phosphoglycerate kinase from Thermotoga maritima reveals the catalytic mechanism and determinants of thermal stability
    • Auerbach, G., Huber, R., Grattinger, M., Zaiss, K., Schurig, H., Jaenicke, R., and Jacob, U. (1997) Closed structure of phosphoglycerate kinase from Thermotoga maritima reveals the catalytic mechanism and determinants of thermal stability, Structure 5, 1475-1483.
    • (1997) Structure , vol.5 , pp. 1475-1483
    • Auerbach, G.1    Huber, R.2    Grattinger, M.3    Zaiss, K.4    Schurig, H.5    Jaenicke, R.6    Jacob, U.7
  • 8
    • 0031030767 scopus 로고    scopus 로고
    • Synergistic effects of substrate-induced conformational changes in phosphoglycerate kinse activation
    • Bernstein, B. E., Michels, P. A. M., and Hol, W. G. J. (1997) Synergistic effects of substrate-induced conformational changes in phosphoglycerate kinse activation, Nature 385, 275-278.
    • (1997) Nature , vol.385 , pp. 275-278
    • Bernstein, B.E.1    Michels, P.A.M.2    Hol, W.G.J.3
  • 9
    • 0032584315 scopus 로고    scopus 로고
    • Crystal structures of substrates and products bound to the phosphoglycerate kinase active site reveal the catalytic mechanism
    • Bernstein, B. E., and Hol, W. G. J. (1998) Crystal structures of substrates and products bound to the phosphoglycerate kinase active site reveal the catalytic mechanism, Biochemistry 37, 4429-4436.
    • (1998) Biochemistry , vol.37 , pp. 4429-4436
    • Bernstein, B.E.1    Hol, W.G.J.2
  • 10
    • 12144285772 scopus 로고    scopus 로고
    • Role of phosphate chain mobility of MgATP in completing the 3-phosphoglycerate kinase catalytic site: Binding, kinetic, and crystallographic studies with ATP and MgATP
    • Flachner, B., Kovari, Z., Varga, A., Gugolya, Z., Vonderviszt, F., Naray-Szabo, G., and Vas, M. (2004) 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, 3436-3449.
    • (2004) Biochemistry , vol.43 , pp. 3436-3449
    • Flachner, B.1    Kovari, Z.2    Varga, A.3    Gugolya, Z.4    Vonderviszt, F.5    Naray-Szabo, G.6    Vas, M.7
  • 11
    • 0037118690 scopus 로고    scopus 로고
    • Crystallographic and thiol-reactivity studies on the complex of pig muscle phosphoglycerate kinase with ATP analogues: Correlation between nucleotide binding mode and helix flexibility
    • Kovari, Z., Flachner, B., Naray-Szabo, G., and Vas, M. (2002) Crystallographic and thiol-reactivity studies on the complex of pig muscle phosphoglycerate kinase with ATP analogues: Correlation between nucleotide binding mode and helix flexibility, Biochemistry 41, 8796-8806.
    • (2002) Biochemistry , vol.41 , pp. 8796-8806
    • Kovari, Z.1    Flachner, B.2    Naray-Szabo, G.3    Vas, M.4
  • 12
    • 18844477875 scopus 로고    scopus 로고
    • Protein conformer selection by sequence-dependent packing contacts in crystals of 3-phosphoglycerate kinase
    • Kovari, Z., and Vas, M. (2004) Protein conformer selection by sequence-dependent packing contacts in crystals of 3-phosphoglycerate kinase, Proteins 55, 198-209.
    • (2004) Proteins , vol.55 , pp. 198-209
    • Kovari, Z.1    Vas, M.2
  • 13
    • 0030095921 scopus 로고    scopus 로고
    • 2.0 Å Resolution structure of a ternary complex of pig muscle phosphoglycerate kinase containing 3-phospho-D-glycerate and the nucleotide Mn adenylylimidodiphosphate
    • May, A., Vas, M., Harlos, K., and Blake, C. (1996) 2.0 Å Resolution structure of a ternary complex of pig muscle phosphoglycerate kinase containing 3-phospho-D-glycerate and the nucleotide Mn adenylylimidodiphosphate, Proteins 24, 292-303.
    • (1996) Proteins , vol.24 , pp. 292-303
    • May, A.1    Vas, M.2    Harlos, K.3    Blake, C.4
  • 14
    • 0026536746 scopus 로고
    • Crystal Structure of the binary complex of pig muscle phosphoglycerate kinse and its substrate 3-phosphoglycerate
    • Harlos, K., Vas, M., and Blake, C. F. (1992) Crystal Structure of the binary complex of pig muscle phosphoglycerate kinse and its substrate 3-phosphoglycerate, Proteins 12, 133-144.
    • (1992) Proteins , vol.12 , pp. 133-144
    • Harlos, K.1    Vas, M.2    Blake, C.F.3
  • 15
    • 0027177819 scopus 로고
    • The anatomy of a kinase and the control of phosphate transfer
    • Joao, H. C., and Williams, R. J. P. (1993) The anatomy of a kinase and the control of phosphate transfer, Eur. J. Biochem. 216, 1-18.
    • (1993) Eur. J. Biochem , vol.216 , pp. 1-18
    • Joao, H.C.1    Williams, R.J.P.2
  • 16
    • 0023902301 scopus 로고
    • NMR analysis of the interdomain region of yeast phosphoglycerate kinase
    • Wilson, H. R., Williams, R. J. P., Littlechild, J. A., and Watson, H. C. (1988) NMR analysis of the interdomain region of yeast phosphoglycerate kinase, Eur. J. Biochem. 170, 529-538.
    • (1988) Eur. J. Biochem , vol.170 , pp. 529-538
    • Wilson, H.R.1    Williams, R.J.P.2    Littlechild, J.A.3    Watson, H.C.4
  • 17
    • 0017278755 scopus 로고
    • Nuclear-magnetic-resonance study of the active-site structure of yeast phosphoglycerate kinase
    • Tanswell, P., Westhead, E. W., and Williams, R. J. P. (1976) Nuclear-magnetic-resonance study of the active-site structure of yeast phosphoglycerate kinase, Eur. J. Biochem. 63, 249-262.
    • (1976) Eur. J. Biochem , vol.63 , pp. 249-262
    • Tanswell, P.1    Westhead, E.W.2    Williams, R.J.P.3
  • 18
    • 0025336465 scopus 로고
    • An NMR study of anion binding to yeast phosphoglycerate kinase
    • Fairbrother, W. J., Graham, H. C., and Williams, R. J. P. (1990) An NMR study of anion binding to yeast phosphoglycerate kinase, Eur. J. Biochem. 190, 161-169.
    • (1990) Eur. J. Biochem , vol.190 , pp. 161-169
    • Fairbrother, W.J.1    Graham, H.C.2    Williams, R.J.P.3
  • 19
    • 0024405187 scopus 로고
    • NMR analysis of site-specific mutants of yeast phosphoglycerate kinase: An investigation of the triose-binding site
    • Fairbrother, W. J., Walker, P. A., Minard, P., Littlechild, J. A., Watson, H. C., and Williams, R. J. P. (1989) NMR analysis of site-specific mutants of yeast phosphoglycerate kinase: An investigation of the triose-binding site, Eur. J. Biochem. 183, 57-67.
    • (1989) Eur. J. Biochem , vol.183 , pp. 57-67
    • Fairbrother, W.J.1    Walker, P.A.2    Minard, P.3    Littlechild, J.A.4    Watson, H.C.5    Williams, R.J.P.6
  • 20
    • 0027049247 scopus 로고
    • Characterization of the structure and properties of the His62→Ala and Arg38→Ala mutants of yeast phosphoglycerate kinase: An investigation of the catalytic and activatory sites by site-directed mutagenesis and NMR
    • Sherman, M. A., Fairbrother, W. J., and Mas, M. T. (1992) Characterization of the structure and properties of the His62→Ala and Arg38→Ala mutants of yeast phosphoglycerate kinase: An investigation of the catalytic and activatory sites by site-directed mutagenesis and NMR, Protein Sci. 1, 752-760.
    • (1992) Protein Sci , vol.1 , pp. 752-760
    • Sherman, M.A.1    Fairbrother, W.J.2    Mas, M.T.3
  • 21
    • 0018606116 scopus 로고
    • Substrate binding closes the cleft between the domains of yeast phosphoglycerate kinase
    • Pickover, C. A., McKay, D. B., Engelman, D. M., and Steitz, T. A. (1979) Substrate binding closes the cleft between the domains of yeast phosphoglycerate kinase, J. Biol. Chem. 254, 11323-11329.
    • (1979) J. Biol. Chem , vol.254 , pp. 11323-11329
    • Pickover, C.A.1    McKay, D.B.2    Engelman, D.M.3    Steitz, T.A.4
  • 22
    • 0036880493 scopus 로고    scopus 로고
    • What vibrations tell us about proteins
    • Barth, A., and Zscherp, C. (2002) What vibrations tell us about proteins, Q. Rev. Biophys. 35, 369-430.
    • (2002) Q. Rev. Biophys , vol.35 , pp. 369-430
    • Barth, A.1    Zscherp, C.2
  • 23
    • 0034698276 scopus 로고    scopus 로고
    • Substrate binding and enzyme function investigated by infrared spectroscopy
    • Barth, A., and Zscherp, C. (2000) Substrate binding and enzyme function investigated by infrared spectroscopy, FEBS Lett. 477, 151-156.
    • (2000) FEBS Lett , vol.477 , pp. 151-156
    • Barth, A.1    Zscherp, C.2
  • 24
    • 0028871804 scopus 로고
    • How to measure and predict the molar absorption coefficient of a protein
    • Pace, C. N., Vajdos, F., Fee, L., Grimsley, G., and Gray, T. (1995) How to measure and predict the molar absorption coefficient of a protein, Protein Sci. 4, 2411-2423.
    • (1995) Protein Sci , vol.4 , pp. 2411-2423
    • Pace, C.N.1    Vajdos, F.2    Fee, L.3    Grimsley, G.4    Gray, T.5
  • 25
    • 0017871989 scopus 로고
    • The steady-state kinetics of yeast phosphoglycerate kinase: Anomalous kinetic plots and the effects of salts on activity
    • Scopes, R. K. (1978) The steady-state kinetics of yeast phosphoglycerate kinase: Anomalous kinetic plots and the effects of salts on activity, Eur. J. Biochem. 85, 503-516.
    • (1978) Eur. J. Biochem , vol.85 , pp. 503-516
    • Scopes, R.K.1
  • 26
    • 22244486662 scopus 로고    scopus 로고
    • Difference FTIR studies reveal nitrogen-containing amino acid side chains are involved in the allosteric regulation of RecA
    • Schwartz, C. M., Drown, P. M., and MacDonald, G. (2005) Difference FTIR studies reveal nitrogen-containing amino acid side chains are involved in the allosteric regulation of RecA, Biochemistry 44, 9733-9745.
    • (2005) Biochemistry , vol.44 , pp. 9733-9745
    • Schwartz, C.M.1    Drown, P.M.2    MacDonald, G.3
  • 27
    • 0026030935 scopus 로고
    • Infrared spectroscopic signals arising from ligand binding and conformational changes in the catalytic cycle of sarcoplasmic reticulum calcium ATPase
    • Barth, A., Mantele, W., and Kreutz, W. (1991) Infrared spectroscopic signals arising from ligand binding and conformational changes in the catalytic cycle of sarcoplasmic reticulum calcium ATPase, Biochim. Biophys. Acta 1057, 115-123.
    • (1991) Biochim. Biophys. Acta , vol.1057 , pp. 115-123
    • Barth, A.1    Mantele, W.2    Kreutz, W.3
  • 28
    • 0027234028 scopus 로고
    • 2+ affects the binding of ADP but not ATP to 3-phosphoglycerate kinase: Correlation between equilibrium dialysis binding and enyme kinetic data
    • 2+ affects the binding of ADP but not ATP to 3-phosphoglycerate kinase: Correlation between equilibrium dialysis binding and enyme kinetic data, Biochem. J. 293, 595-599.
    • (1993) Biochem. J , vol.293 , pp. 595-599
    • Molnar, M.1    Vas, M.2
  • 29
    • 0346381003 scopus 로고
    • Activation of yeast phosphoglycerate kinase by salts of monovalent cations
    • Larsson-Raznikiewicz, M., and Jansson, J. R. (1973) Activation of yeast phosphoglycerate kinase by salts of monovalent cations, FEBS Lett. 29, 345-347.
    • (1973) FEBS Lett , vol.29 , pp. 345-347
    • Larsson-Raznikiewicz, M.1    Jansson, J.R.2
  • 30
    • 0029018548 scopus 로고
    • The use and misuse of FTIR spectroscopy in the determination of protein structure
    • Jackson, M., and Mantsch, H. H. (1995) The use and misuse of FTIR spectroscopy in the determination of protein structure, Crit. Rev. Biochem. Mol. Biol. 30, 95-120.
    • (1995) Crit. Rev. Biochem. Mol. Biol , vol.30 , pp. 95-120
    • Jackson, M.1    Mantsch, H.H.2
  • 31
    • 0034473318 scopus 로고    scopus 로고
    • The infrared absorption of amino acid side chains
    • Barth, A. (2000) The infrared absorption of amino acid side chains, Prog. Biophys. Mol. Biol. 74, 141-173.
    • (2000) Prog. Biophys. Mol. Biol , vol.74 , pp. 141-173
    • Barth, A.1
  • 32
    • 0029349392 scopus 로고
    • A comparative study of ATP and GTP complexation with trivalent Al, Ga and Fe cations. Determination of cation binding site and nucleotide conformation by FTIR difference spectroscopy
    • El-Mahdaoui, L., and Tajmir-Riahi, H. A. (1995) A comparative study of ATP and GTP complexation with trivalent Al, Ga and Fe cations. Determination of cation binding site and nucleotide conformation by FTIR difference spectroscopy, J. Biomol. Struct. Dyn. 13, 69-86.
    • (1995) J. Biomol. Struct. Dyn , vol.13 , pp. 69-86
    • El-Mahdaoui, L.1    Tajmir-Riahi, H.A.2
  • 33
    • 0025613794 scopus 로고
    • 2O) solutions. I. Spectral parameters of amino acid residue absorption bands
    • 2O) solutions. I. Spectral parameters of amino acid residue absorption bands, Biopolymers 30, 1243-1257.
    • (1990) Biopolymers , vol.30 , pp. 1243-1257
    • Venyaminov, S.Y.1    Kalnin, N.N.2
  • 34
    • 0025157643 scopus 로고
    • Proline residues undergo structural changes during proton pumping in bacteriorhodopsin
    • Gerwert, K., Hess, B., and Englehard, M. (1990) Proline residues undergo structural changes during proton pumping in bacteriorhodopsin, FEBS Lett. 261, 449-454.
    • (1990) FEBS Lett , vol.261 , pp. 449-454
    • Gerwert, K.1    Hess, B.2    Englehard, M.3
  • 36
    • 29344443515 scopus 로고    scopus 로고
    • Substrate-assisted movement of the catalytic Lys 215 during domain closure: Site-directed mutagenesis studies of human 3-phosphoglycerate kinase
    • Flachner, B., Varga, A., Szabo, J., Barna, L., Hajdu, I., Gyimesi, G., Zavodszky, P., and Vas, M. (2005) Substrate-assisted movement of the catalytic Lys 215 during domain closure: Site-directed mutagenesis studies of human 3-phosphoglycerate kinase, Biochemistry 44, 16853-16865.
    • (2005) Biochemistry , vol.44 , pp. 16853-16865
    • Flachner, B.1    Varga, A.2    Szabo, J.3    Barna, L.4    Hajdu, I.5    Gyimesi, G.6    Zavodszky, P.7    Vas, M.8


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.