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Volumn 46, Issue 19, 2007, Pages 5722-5731

Crystal structure of a hyperactive Escherichia coli glycerol kinase mutant Gly230 → Asp obtained using microfluidic crystallization devices

Author keywords

[No Author keywords available]

Indexed keywords

CRYSTAL STRUCTURE; CRYSTALLIZATION; ESCHERICHIA COLI; GLYCEROL; MICROFLUIDICS; MUTAGENS;

EID: 34248585864     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi700096p     Document Type: Article
Times cited : (26)

References (39)
  • 1
    • 0037079023 scopus 로고    scopus 로고
    • Escherichia coli K-12 undergoes adaptive evolution to achieve in silico predicted optimal growth
    • Ibarra, R. U., Edwards, J. S., and Palsson, B. O. (2002) Escherichia coli K-12 undergoes adaptive evolution to achieve in silico predicted optimal growth, Nature 420, 186-189.
    • (2002) Nature , vol.420 , pp. 186-189
    • Ibarra, R.U.1    Edwards, J.S.2    Palsson, B.O.3
  • 2
    • 10944220879 scopus 로고    scopus 로고
    • High-throughput mutation detection underlying adaptive evolution of Escherichia coli-K12
    • Honisch, C., Raghunathan, A., Cantor, C. R., Palsson, B. O., and van den Boom, D. (2004) High-throughput mutation detection underlying adaptive evolution of Escherichia coli-K12, Genome Res. 14, 2495-2502.
    • (2004) Genome Res , vol.14 , pp. 2495-2502
    • Honisch, C.1    Raghunathan, A.2    Cantor, C.R.3    Palsson, B.O.4    van den Boom, D.5
  • 4
    • 0014802916 scopus 로고
    • Glycerol kinase, the pacemaker for the dissimilation of glycerol in Escherichia coli
    • Zwaig, N., Kistler, W. S., and Lin, E. C. C. (1970) Glycerol kinase, the pacemaker for the dissimilation of glycerol in Escherichia coli, J. Bacteriol. 102, 753-759.
    • (1970) J. Bacteriol , vol.102 , pp. 753-759
    • Zwaig, N.1    Kistler, W.S.2    Lin, E.C.C.3
  • 5
    • 0011377510 scopus 로고
    • Utilization of L-α-glycerophosphate by Escherichia coli without hydrolysis
    • Lin, E. C. C., Koch, J. P., Chused, T. M., and Jorgensen, S. E. (1962) Utilization of L-α-glycerophosphate by Escherichia coli without hydrolysis, Proc. Nat. Acad. Sci. U.S.A. 48, 2145-2150.
    • (1962) Proc. Nat. Acad. Sci. U.S.A , vol.48 , pp. 2145-2150
    • Lin, E.C.C.1    Koch, J.P.2    Chused, T.M.3    Jorgensen, S.E.4
  • 6
    • 0018070736 scopus 로고
    • Subunit dissociation in the allosteric regulation of glycerol kinase from Escherichia coli. 1. Kinetic evidence
    • de Riel, J. K., and Paulus, H. (1978a) Subunit dissociation in the allosteric regulation of glycerol kinase from Escherichia coli. 1. Kinetic evidence, Biochemistry 17, 5134-5140.
    • (1978) Biochemistry , vol.17 , pp. 5134-5140
    • de Riel, J.K.1    Paulus, H.2
  • 7
    • 0018069679 scopus 로고
    • Subunit dissociation in the allosteric regulation of glycerol kinase from Escherichia coli. 2. Physical evidence
    • de Riel, J. K., and Paulus, H. (1978b) Subunit dissociation in the allosteric regulation of glycerol kinase from Escherichia coli. 2. Physical evidence, Biochemistry 17, 5141-5145.
    • (1978) Biochemistry , vol.17 , pp. 5141-5145
    • de Riel, J.K.1    Paulus, H.2
  • 8
    • 0018141201 scopus 로고
    • Subunit dissociation in the allosteric regulation of glycerol kinase from Escherichia coli. 3. Role in desensitization
    • de Riel, J. K., and Paulus, H. (1978c) Subunit dissociation in the allosteric regulation of glycerol kinase from Escherichia coli. 3. Role in desensitization, Biochemistry 17, 5146-5150.
    • (1978) Biochemistry , vol.17 , pp. 5146-5150
    • de Riel, J.K.1    Paulus, H.2
  • 9
    • 0025166757 scopus 로고
    • Nucleotide regulation of Escherichia coli glycerol kinase: Initial-velocity and substrate binding studies
    • Pettigrew, D. W., Yu, G.-J., and Liu, Y. (1990) Nucleotide regulation of Escherichia coli glycerol kinase: initial-velocity and substrate binding studies, Biochemistry 29, 8620-8627.
    • (1990) Biochemistry , vol.29 , pp. 8620-8627
    • Pettigrew, D.W.1    Yu, G.-J.2    Liu, Y.3
  • 10
    • 0029948487 scopus 로고    scopus 로고
    • The sugar kinase/heat shock protein 70/actin superfamily: Implications of conserved structure for mechanism
    • Hurley, J. H. (1996) The sugar kinase/heat shock protein 70/actin superfamily: implications of conserved structure for mechanism, Annu. Rev. Biophys. Biomol. Struct. 25, 137-162.
    • (1996) Annu. Rev. Biophys. Biomol. Struct , vol.25 , pp. 137-162
    • Hurley, J.H.1
  • 11
    • 0033596853 scopus 로고    scopus 로고
    • Crystal structure of Escherichia coli glycerol kinase variant S58 → W in complex with nonhydrolyzable ATP analogues reveal a putative active conformation of the enzyme as a result of domain motion
    • Bystrom, C. E., Pettigrew, D. W., Branchaud, B. P., O'Brien, P., and Remington, S. J. (1999) Crystal structure of Escherichia coli glycerol kinase variant S58 → W in complex with nonhydrolyzable ATP analogues reveal a putative active conformation of the enzyme as a result of domain motion, Biochemistry 38, 3508-3518.
    • (1999) Biochemistry , vol.38 , pp. 3508-3518
    • Bystrom, C.E.1    Pettigrew, D.W.2    Branchaud, B.P.3    O'Brien, P.4    Remington, S.J.5
  • 12
    • 0015875125 scopus 로고
    • Catalytic and allosteric properties of glycerol kinase from Escherichia coli
    • Thorner, J. W., and Paulus, H. (1973) Catalytic and allosteric properties of glycerol kinase from Escherichia coli, J. Biol. Chem. 248, 3922-3932.
    • (1973) J. Biol. Chem , vol.248 , pp. 3922-3932
    • Thorner, J.W.1    Paulus, H.2
  • 13
    • 0000539364 scopus 로고
    • Glucose-induced conformational change in yeast hexokinase
    • Bennett Jr., W. S., and Steitz, T. A. (1978) Glucose-induced conformational change in yeast hexokinase, Proc. Natl. Acad. Sci. U.S.A. 75, 4848-4852.
    • (1978) Proc. Natl. Acad. Sci. U.S.A , vol.75 , pp. 4848-4852
    • Bennett Jr., W.S.1    Steitz, T.A.2
  • 14
    • 0030575783 scopus 로고    scopus 로고
    • The structure of an open state of b-actin at 265 Å resolution
    • Chik, J. K., Lindberg, U., and Schutt, C. E. (1996) The structure of an open state of b-actin at 265 Å resolution, J. Mol. Biol. 263, 607-623.
    • (1996) J. Mol. Biol , vol.263 , pp. 607-623
    • Chik, J.K.1    Lindberg, U.2    Schutt, C.E.3
  • 15
    • 0021288128 scopus 로고
    • Glc of the phosphoenolpyruvate: Sugar phosphotransferase system and glycerol kinase of Salmonella typhimurium
    • Glc of the phosphoenolpyruvate: sugar phosphotransferase system and glycerol kinase of Salmonella typhimurium, J. Bacteriol. 158, 351-353.
    • (1984) J. Bacteriol , vol.158 , pp. 351-353
    • Postma, P.W.1    Epstein, W.2    Schuitema, A.R.J.3    Nelson, S.O.4
  • 17
    • 0014013188 scopus 로고
    • Feedback inhibition of glycerol kinase, a catabolic enzyme in Escherichia coli
    • Zwaig, N., and Lin, E. C. C. (1966) Feedback inhibition of glycerol kinase, a catabolic enzyme in Escherichia coli, Science 153, 755-757.
    • (1966) Science , vol.153 , pp. 755-757
    • Zwaig, N.1    Lin, E.C.C.2
  • 19
    • 0032533833 scopus 로고    scopus 로고
    • Glycerol kinase from Escherichia coli and an Ala65 → Thr mutant: The crystal structures reveal conformational changes with implications for allosteric regulation
    • Feese, M. D., Faber, H. R., Bystrom, C. E., Pettigrew, D. W., and Remington, S. J. (1998) Glycerol kinase from Escherichia coli and an Ala65 → Thr mutant: the crystal structures reveal conformational changes with implications for allosteric regulation, Structure 6, 1407-1418.
    • (1998) Structure , vol.6 , pp. 1407-1418
    • Feese, M.D.1    Faber, H.R.2    Bystrom, C.E.3    Pettigrew, D.W.4    Remington, S.J.5
  • 20
    • 0032564319 scopus 로고    scopus 로고
    • Crystal structure of a complex of Escherichia coli glycerol kinase and an allosteric effector fructose 1,6-bisphosphate
    • Ormo, M. O., Bystrom, C. E., and Remington, S. J. (1998) Crystal structure of a complex of Escherichia coli glycerol kinase and an allosteric effector fructose 1,6-bisphosphate, Biochemistry 37, 16565-16572.
    • (1998) Biochemistry , vol.37 , pp. 16565-16572
    • Ormo, M.O.1    Bystrom, C.E.2    Remington, S.J.3
  • 21
    • 0023879283 scopus 로고
    • Escherichia coli glycerol kinase. Cloning and sequencing of the glpK gene and the primary structure of the enzyme
    • Pettigrew, D. W., Ma, D. P., Conrad, C. A., and Johnson, J. R. (1988) Escherichia coli glycerol kinase. Cloning and sequencing of the glpK gene and the primary structure of the enzyme, J. Biol. Chem. 263, 135-139.
    • (1988) J. Biol. Chem , vol.263 , pp. 135-139
    • Pettigrew, D.W.1    Ma, D.P.2    Conrad, C.A.3    Johnson, J.R.4
  • 22
    • 0345643778 scopus 로고    scopus 로고
    • A single amino acid change in Escherichia coli glycerol kinase abolishes glucose control of glycerol utilization in vivo
    • Pettigrew, D., Liu, W., Holmes, C., Meadow, N., and Roseman, S. (1996) A single amino acid change in Escherichia coli glycerol kinase abolishes glucose control of glycerol utilization in vivo, J. Bacteriol. 178, 2846-2852.
    • (1996) J. Bacteriol , vol.178 , pp. 2846-2852
    • Pettigrew, D.1    Liu, W.2    Holmes, C.3    Meadow, N.4    Roseman, S.5
  • 24
    • 0024403235 scopus 로고
    • Crystallization and preliminary X-ray studies of Escherichia coli glycerol kinase
    • Faber, H. R., Pettigrew, D. W., and Remington, S. J. (1989) Crystallization and preliminary X-ray studies of Escherichia coli glycerol kinase, J. Mol. Biol. 207, 637-639.
    • (1989) J. Mol. Biol , vol.207 , pp. 637-639
    • Faber, H.R.1    Pettigrew, D.W.2    Remington, S.J.3
  • 25
    • 22144457451 scopus 로고    scopus 로고
    • Multiple-mutation reaction: A method for simultaneous introduction of multiple mutations into the glpK gene of Mycoplasma pneumoniae
    • Hames, C., Halbedel, S., Schilling, O., and Stulke, J. (2005) Multiple-mutation reaction: a method for simultaneous introduction of multiple mutations into the glpK gene of Mycoplasma pneumoniae, Appl. Environ. Microbiol. 71, 4097-4100.
    • (2005) Appl. Environ. Microbiol , vol.71 , pp. 4097-4100
    • Hames, C.1    Halbedel, S.2    Schilling, O.3    Stulke, J.4
  • 26
    • 0027498262 scopus 로고
    • Light scattering and the absolute characterization of macromolecules
    • Wyatt, P. J. (1993) Light scattering and the absolute characterization of macromolecules, Anal. Chim. Acta 272, 1-40.
    • (1993) Anal. Chim. Acta , vol.272 , pp. 1-40
    • Wyatt, P.J.1
  • 27
    • 0029862811 scopus 로고    scopus 로고
    • Assembly of the gigantic hemoglobin of the earthworm Lumbricus terrestris
    • Zhu, H., Ownby, D. W., Riggs, C. K., Nolasco, N. J., Stoops, J. K., and Riggs, A. F. (1996) Assembly of the gigantic hemoglobin of the earthworm Lumbricus terrestris, J. Biol. Chem. 271, 30007-30021.
    • (1996) J. Biol. Chem , vol.271 , pp. 30007-30021
    • Zhu, H.1    Ownby, D.W.2    Riggs, C.K.3    Nolasco, N.J.4    Stoops, J.K.5    Riggs, A.F.6
  • 28
    • 5144223105 scopus 로고    scopus 로고
    • Systematic investigation of protein phase behavior with a microfluidic formulator
    • Hansen, C. L., Sommer, M. O. A., and Quake, S. R. (2004) Systematic investigation of protein phase behavior with a microfluidic formulator, Proc. Natl. Acad. Sci. U.S.A. 101, 14431-14436.
    • (2004) Proc. Natl. Acad. Sci. U.S.A , vol.101 , pp. 14431-14436
    • Hansen, C.L.1    Sommer, M.O.A.2    Quake, S.R.3
  • 29
    • 33750953828 scopus 로고    scopus 로고
    • Phase knowledge enables rational screens for protein crystallization
    • Anderson, M. J., Hansen, C. L., and Quake, S. R. (2006) Phase knowledge enables rational screens for protein crystallization, Proc. Nat. Acad. Sci. U.S.A. 103, 16746-16751.
    • (2006) Proc. Nat. Acad. Sci. U.S.A , vol.103 , pp. 16746-16751
    • Anderson, M.J.1    Hansen, C.L.2    Quake, S.R.3
  • 30
    • 33644962807 scopus 로고    scopus 로고
    • A microfluidic device for kinetic optimization of protein crystallization and in situ structure determination
    • Hansen, C. L., Classen, S., Berger, J. M., and Quake, S. R. (2006) A microfluidic device for kinetic optimization of protein crystallization and in situ structure determination, J. Am. Chem. Soc. 128, 3142-3143.
    • (2006) J. Am. Chem. Soc , vol.128 , pp. 3142-3143
    • Hansen, C.L.1    Classen, S.2    Berger, J.M.3    Quake, S.R.4
  • 31
    • 0031059866 scopus 로고    scopus 로고
    • Processing X-ray diffraction data collection in oscillation mode
    • Otwinowski, Z., and Minor, W. (1997) Processing X-ray diffraction data collection in oscillation mode, Methods Enzymol. 276, 307-326.
    • (1997) Methods Enzymol , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 33
    • 84889120137 scopus 로고
    • Improved methods for building protein models in electron density maps and the location of errors in these models
    • Jones, T. A., Zou, J.-Y., Cowan, S. W., and Kjeldgaard, M. (1991) Improved methods for building protein models in electron density maps and the location of errors in these models, Acta Crystallogr. A47, 110-119.
    • (1991) Acta Crystallogr , vol.A47 , pp. 110-119
    • Jones, T.A.1    Zou, J.-Y.2    Cowan, S.W.3    Kjeldgaard, M.4
  • 35
    • 0035182073 scopus 로고    scopus 로고
    • Use of TLS parameters to model anisotropic displacements in macromolecular refinement
    • Winn, M. D., Isupov, M. N., and Murshudov, G. N. (2001) Use of TLS parameters to model anisotropic displacements in macromolecular refinement, Acta Crystallogr. D57, 122-133.
    • (2001) Acta Crystallogr , vol.D57 , pp. 122-133
    • Winn, M.D.1    Isupov, M.N.2    Murshudov, G.N.3
  • 36
    • 0030883755 scopus 로고    scopus 로고
    • Protein domain movements: Detection of rigid domains and visualization of hinges in comparisons of atomic coordinates
    • Wriggers, W., and Schulten, K. (1997) Protein domain movements: detection of rigid domains and visualization of hinges in comparisons of atomic coordinates, Proteins: Struct., Funct., Genet. 29, 1-14.
    • (1997) Proteins: Struct., Funct., Genet , vol.29 , pp. 1-14
    • Wriggers, W.1    Schulten, K.2
  • 37
    • 0037168508 scopus 로고    scopus 로고
    • A robust and scalable microfluidic metering method that allows protein crystal growth by free interface diffusion
    • Hansen, C. L., Skordalakes, E., Berger, J. M., and Quake, S. R. (2002) A robust and scalable microfluidic metering method that allows protein crystal growth by free interface diffusion, Proc. Natl. Acad. Sci. U.S.A. 99, 16531-16536.
    • (2002) Proc. Natl. Acad. Sci. U.S.A , vol.99 , pp. 16531-16536
    • Hansen, C.L.1    Skordalakes, E.2    Berger, J.M.3    Quake, S.R.4
  • 38
    • 0001897686 scopus 로고
    • Assessment of phase accuracy by cross validation: The free R value
    • Brunger, A. (1993) Assessment of phase accuracy by cross validation: the free R value, Acta Crystallogr. D49, 24-36.
    • (1993) Acta Crystallogr , vol.D49 , pp. 24-36
    • Brunger, A.1


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