메뉴 건너뛰기




Volumn 429, Issue 2, 2010, Pages 313-321

Mutation of outer-shell residues modulates metal ion co-ordination strength in a metalloenzyme

Author keywords

Directed evolution; Metal ion binding; Metal ion co ordination; Phosphotriesterase (PTE)

Indexed keywords

ACTIVE SITE; AGROBACTERIUM RADIOBACTER; BIOCHEMICAL PROPERTIES; CONFORMATIONAL STATE; DIRECTED EVOLUTION; ESSENTIAL SUPPORT; METAL ION BINDING; METAL ION INTERACTIONS; METALLO-PROTEINS; METALLOENZYMES; MODEL SYSTEM; OPTIMAL ORIENTATION; ORTHOLOGUES; PHOSPHOTRIESTERASES; PROTEIN FOLDS; PSEUDOMONAS DIMINUTA; SMALL MOLECULES; SPECTROSCOPIC TECHNIQUE; STABILIZING EFFECTS; STRUCTURAL DATA; STRUCTURAL DETERMINANTS;

EID: 77954739001     PISSN: 02646021     EISSN: 14708728     Source Type: Journal    
DOI: 10.1042/BJ20100233     Document Type: Article
Times cited : (17)

References (46)
  • 1
    • 57649207910 scopus 로고    scopus 로고
    • How do bacterial cells ensure that metalloproteins get the correct metal?
    • Waldron, K. J. and Robinson, N. J. (2009) How do bacterial cells ensure that metalloproteins get the correct metal? Nat. Rev. Microbiol. 7, 25-35
    • (2009) Nat. Rev. Microbiol. , vol.7 , pp. 25-35
    • Waldron, K.J.1    Robinson, N.J.2
  • 2
    • 0026410002 scopus 로고
    • Structural aspects of metal liganding to functional groups in proteins
    • Glusker, J. P. (1991) Structural aspects of metal liganding to functional groups in proteins. Adv. Protein Chem. 42, 1-76
    • (1991) Adv. Protein Chem. , vol.42 , pp. 1-76
    • Glusker, J.P.1
  • 3
    • 0030504446 scopus 로고    scopus 로고
    • The nature of the coordination sites of transition metals in proteins
    • Garner, C. D., Collison, D. and Pidcock, E. (1996) The nature of the coordination sites of transition metals in proteins. Philos. Trans. R. Soc. A. 354, 325-357
    • (1996) Philos. Trans. R. Soc. A , vol.354 , pp. 325-357
    • Garner, C.D.1    Collison, D.2    Pidcock, E.3
  • 4
    • 0030053257 scopus 로고    scopus 로고
    • An isoleucine to leucine mutation that switches the cofactor requirement of the EcoRV restriction endonuclease from magnesium to manganese
    • Vipond, I. B., Moon, B. J. and Halford, S. E. (1996) An isoleucine to leucine mutation that switches the cofactor requirement of the EcoRV restriction endonuclease from magnesium to manganese. Biochemistry 35, 1712-1721
    • (1996) Biochemistry , vol.35 , pp. 1712-1721
    • Vipond, I.B.1    Moon, B.J.2    Halford, S.E.3
  • 5
    • 0347130091 scopus 로고    scopus 로고
    • Growth of Escherichia coli coexpressing phosphotriesterase and glycerophosphodiester phosphodiesterase, using paraoxon as the sole phosphorus source
    • McLoughlin, S. Y., Jackson, C., Liu, J. W. and Ollis, D. L. (2004) Growth of Escherichia coli coexpressing phosphotriesterase and glycerophosphodiester phosphodiesterase, using paraoxon as the sole phosphorus source. Appl. Environ. Microbiol. 70, 404-412
    • (2004) Appl. Environ. Microbiol. , vol.70 , pp. 404-412
    • McLoughlin, S.Y.1    Jackson, C.2    Liu, J.W.3    Ollis, D.L.4
  • 6
    • 33847789468 scopus 로고    scopus 로고
    • The structure and function of a novel glycerophosphodiesterase from Enterobacter aerogenes
    • Jackson, C. J., Carr, P. D., Liu, J. W., Watt, S. J., Beck, J. L. and Ollis, D. L. (2007) The structure and function of a novel glycerophosphodiesterase from Enterobacter aerogenes. J. Mol. Biol. 367, 1047-1062
    • (2007) J. Mol. Biol. , vol.367 , pp. 1047-1062
    • Jackson, C.J.1    Carr, P.D.2    Liu, J.W.3    Watt, S.J.4    Beck, J.L.5    Ollis, D.L.6
  • 7
    • 69049087726 scopus 로고    scopus 로고
    • Structural flexibility enhances the reactivity of the bioremediator glycerophosphodiesterase by fine-tuning its mechanism of hydrolysis
    • Hadler, K. S., Mitic, N., Ely, F., Hanson, G. R., Gahan, L. R., Larrabee, J. A., Ollis, D. L. and Schenk, G. (2009) Structural flexibility enhances the reactivity of the bioremediator glycerophosphodiesterase by fine-tuning its mechanism of hydrolysis. J. Am. Chem. Soc. 131, 11900-11908
    • (2009) J. Am. Chem. Soc. , vol.131 , pp. 11900-11908
    • Hadler, K.S.1    Mitic, N.2    Ely, F.3    Hanson, G.R.4    Gahan, L.R.5    Larrabee, J.A.6    Ollis, D.L.7    Schenk, G.8
  • 8
    • 0034671767 scopus 로고    scopus 로고
    • Calcium affinity of regulatory sites in skeletal troponin-C is attenuated by N-cap mutations of helix C
    • Leblanc, L., Bennet, A. and Borgford, T. (2000) Calcium affinity of regulatory sites in skeletal troponin-C is attenuated by N-cap mutations of helix C. Arch. Biochem. Biophys. 384, 296-304
    • (2000) Arch. Biochem. Biophys. , vol.384 , pp. 296-304
    • Leblanc, L.1    Bennet, A.2    Borgford, T.3
  • 11
    • 0024332036 scopus 로고
    • Parathion hydrolase specified by the flavobacterium opd gene: Relationship between the gene and protein
    • Mulbry, W. W. and Karns, J. S. (1989) Parathion hydrolase specified by the flavobacterium opd gene: relationship between the gene and protein. J. Bacteriol. 171, 6740-6746
    • (1989) J. Bacteriol. , vol.171 , pp. 6740-6746
    • Mulbry, W.W.1    Karns, J.S.2
  • 13
    • 0025836538 scopus 로고
    • Limits of diffusion in the hydrolysis of substrates by the phosphotriesterase from Pseudomonas diminuta
    • Caldwell, S. R., Newcomb, J. R., Schlecht, K. A. and Raushel, F. M. (1991) Limits of diffusion in the hydrolysis of substrates by the phosphotriesterase from Pseudomonas diminuta. Biochemistry 30, 7438-7444
    • (1991) Biochemistry , vol.30 , pp. 7438-7444
    • Caldwell, S.R.1    Newcomb, J.R.2    Schlecht, K.A.3    Raushel, F.M.4
  • 15
  • 17
    • 0025117439 scopus 로고
    • Inactivation of organophosphorus nerve agents by the phosphotriesterase from Pseudomonas diminuta
    • Dumas, D. P., Durst, H. D., Landis, W. G., Raushel, F. M. and Wild, J. R. (1990) Inactivation of organophosphorus nerve agents by the phosphotriesterase from Pseudomonas diminuta. Arch. Biochem. Biophys. 277, 155-159
    • (1990) Arch. Biochem. Biophys. , vol.277 , pp. 155-159
    • Dumas, D.P.1    Durst, H.D.2    Landis, W.G.3    Raushel, F.M.4    Wild, J.R.5
  • 20
    • 0033537687 scopus 로고    scopus 로고
    • Modification of near active site residues in organophosphorus hydrolase reduces metal stoichiometry and alters substrate specificity
    • diSioudi, B., Grimsley, J. K., Lai, K. and Wild, J. R. (1999) Modification of near active site residues in organophosphorus hydrolase reduces metal stoichiometry and alters substrate specificity. Biochemistry 38, 2866-2872
    • (1999) Biochemistry , vol.38 , pp. 2866-2872
    • DiSioudi, B.1    Grimsley, J.K.2    Lai, K.3    Wild, J.R.4
  • 21
    • 0034908590 scopus 로고    scopus 로고
    • Stereoselective detoxification of chiral sarin and soman analogues by phosphotriesterase
    • Li, W. S., Lum, K. T., Chen-Goodspeed, M., Sogorb, M. A. and Raushel, F. M. (2001) Stereoselective detoxification of chiral sarin and soman analogues by phosphotriesterase. Bioorg. Med. Chem. 9, 2083-2091
    • (2001) Bioorg. Med. Chem. , vol.9 , pp. 2083-2091
    • Li, W.S.1    Lum, K.T.2    Chen-Goodspeed, M.3    Sogorb, M.A.4    Raushel, F.M.5
  • 22
    • 0029032588 scopus 로고
    • Three-dimensional structure of the binuclear metal center of phosphotriesterase
    • Benning, M. M., Kuo, J. M., Raushel, F. M. and Holden, H. M. (1995) Three-dimensional structure of the binuclear metal center of phosphotriesterase. Biochemistry 34, 7973-7978
    • (1995) Biochemistry , vol.34 , pp. 7973-7978
    • Benning, M.M.1    Kuo, J.M.2    Raushel, F.M.3    Holden, H.M.4
  • 23
    • 0024316913 scopus 로고
    • Purification and properties of the phosphotriesterase from Pseudomonas diminuta
    • Dumas, D. P., Caldwell, S. R., Wild, J. R. and Raushel, F. M. (1989) Purification and properties of the phosphotriesterase from Pseudomonas diminuta. J. Biol. Chem. 264, 19659-19665
    • (1989) J. Biol. Chem. , vol.264 , pp. 19659-19665
    • Dumas, D.P.1    Caldwell, S.R.2    Wild, J.R.3    Raushel, F.M.4
  • 24
    • 33746934144 scopus 로고    scopus 로고
    • Anomalous scattering analysis of Agrobacterium radiobacter phosphotriesterase: The prominent role of iron in the heterobinuclear active site
    • Jackson, C. J., Carr, P. D., Kim, H. K., Liu, J. W., Herrald, P., Mitic, N., Schenk, G., Smith, C. A. and Ollis, D. L. (2006) Anomalous scattering analysis of Agrobacterium radiobacter phosphotriesterase: the prominent role of iron in the heterobinuclear active site. Biochem. J. 397, 501-508
    • (2006) Biochem. J. , vol.397 , pp. 501-508
    • Jackson, C.J.1    Carr, P.D.2    Kim, H.K.3    Liu, J.W.4    Herrald, P.5    Mitic, N.6    Schenk, G.7    Smith, C.A.8    Ollis, D.L.9
  • 25
    • 0026748791 scopus 로고
    • Characterization of the zinc binding site of bacterial phosphotriesterase
    • Omburo, G. A., Kuo, J. M., Mullins, L. S. and Raushel, F. M. (1992) Characterization of the zinc binding site of bacterial phosphotriesterase. J. Biol. Chem. 267, 13278-13283
    • (1992) J. Biol. Chem. , vol.267 , pp. 13278-13283
    • Omburo, G.A.1    Kuo, J.M.2    Mullins, L.S.3    Raushel, F.M.4
  • 26
    • 0035814923 scopus 로고    scopus 로고
    • High resolution X-ray structures of different metal-substituted forms of phosphotriesterase from Pseudomonas diminuta
    • Benning, M. M., Shim, H., Raushel, F. M. and Holden, H. M. (2001) High resolution X-ray structures of different metal-substituted forms of phosphotriesterase from Pseudomonas diminuta. Biochemistry 40, 2712-2722
    • (2001) Biochemistry , vol.40 , pp. 2712-2722
    • Benning, M.M.1    Shim, H.2    Raushel, F.M.3    Holden, H.M.4
  • 27
    • 0034720769 scopus 로고    scopus 로고
    • Self-assembly of the binuclear metal center of phosphotriesterase
    • DOI 10.1021/bi000291o
    • Shim, H. and Raushel, F. M. (2000) Self-assembly of the binuclear metal center of phosphotriesterase. Biochemistry 39, 7357-7364 (Pubitemid 30422051)
    • (2000) Biochemistry , vol.39 , Issue.25 , pp. 7357-7364
    • Shim, H.1    Raushel, F.M.2
  • 28
    • 2442496666 scopus 로고    scopus 로고
    • Mechanism for the hydrolysis of organophosphates by the bacterial phosphotriesterase
    • Aubert, S. D., Li, Y. and Raushel, F. M. (2004) Mechanism for the hydrolysis of organophosphates by the bacterial phosphotriesterase. Biochemistry 43, 5707-5715
    • (2004) Biochemistry , vol.43 , pp. 5707-5715
    • Aubert, S.D.1    Li, Y.2    Raushel, F.M.3
  • 29
    • 0029759529 scopus 로고    scopus 로고
    • Metal-substrate interactions facilitate the catalytic activity of the bacterial phosphotriesterase
    • Hong, S. B. and Raushel, F. M. (1996) Metal-substrate interactions facilitate the catalytic activity of the bacterial phosphotriesterase. Biochemistry 35, 10904-10912
    • (1996) Biochemistry , vol.35 , pp. 10904-10912
    • Hong, S.B.1    Raushel, F.M.2
  • 30
    • 0343580454 scopus 로고    scopus 로고
    • Perturbations to the active site of phosphotriesterase
    • Kuo, J. M., Chae, M. Y. and Raushel, F. M. (1997) Perturbations to the active site of phosphotriesterase. Biochemistry 36, 1982-1988
    • (1997) Biochemistry , vol.36 , pp. 1982-1988
    • Kuo, J.M.1    Chae, M.Y.2    Raushel, F.M.3
  • 31
    • 13244281317 scopus 로고    scopus 로고
    • Coot: Model-building tools for molecular graphics
    • Emsley, P. and Cowtan, K. (2004) Coot: model-building tools for molecular graphics. Acta Crystallogr. D. 60, 2126-2132
    • (2004) Acta Crystallogr. D , vol.60 , pp. 2126-2132
    • Emsley, P.1    Cowtan, K.2
  • 32
    • 23944485399 scopus 로고    scopus 로고
    • The structure of an enzyme-product complex reveals the critical role of a terminal hydroxide nucleophile in the bacterial phosphotriesterase mechanism
    • Jackson, C., Kim, H. K., Carr, P. D., Liu, J. W. and Ollis, D. L. (2005) The structure of an enzyme-product complex reveals the critical role of a terminal hydroxide nucleophile in the bacterial phosphotriesterase mechanism. Biochim. Biophys. Acta 1752, 56-64
    • (2005) Biochim. Biophys. Acta , vol.1752 , pp. 56-64
    • Jackson, C.1    Kim, H.K.2    Carr, P.D.3    Liu, J.W.4    Ollis, D.L.5
  • 33
    • 0028103275 scopus 로고
    • The CCP4 suite: Programs for protein crystallography
    • Collaborative Computational Project, Number 4
    • Collaborative Computational Project, Number 4 (1994) The CCP4 suite: programs for protein crystallography. Acta Crystallogr. Sect. D Biol. Crystallogr. 50, 760-763
    • (1994) Acta Crystallogr. Sect. D Biol. Crystallogr. , vol.50 , pp. 760-763
  • 34
    • 77954898250 scopus 로고    scopus 로고
    • Reference deleted
    • Reference deleted
  • 35
    • 17144364646 scopus 로고    scopus 로고
    • Directed evolution of phosphotriesterase from Pseudomonas diminuta for heterologous expression in Escherichia coli results in stabilization of the metal-free state
    • Roodveldt, C. and Tawfik, D. S. (2005) Directed evolution of phosphotriesterase from Pseudomonas diminuta for heterologous expression in Escherichia coli results in stabilization of the metal-free state. Protein Eng. Des. Sel. 18, 51-58
    • (2005) Protein Eng. Des. Sel. , vol.18 , pp. 51-58
    • Roodveldt, C.1    Tawfik, D.S.2
  • 36
    • 18144390545 scopus 로고    scopus 로고
    • Increased expression of a bacterial phosphotriesterase in Escherichia coli through directed evolution
    • McLoughlin, S. Y., Jackson, C., Liu, J. W. and Ollis, D. (2005) Increased expression of a bacterial phosphotriesterase in Escherichia coli through directed evolution. Protein Expression Purif. 41, 433-440
    • (2005) Protein Expression Purif. , vol.41 , pp. 433-440
    • McLoughlin, S.Y.1    Jackson, C.2    Liu, J.W.3    Ollis, D.4
  • 37
    • 0035814812 scopus 로고    scopus 로고
    • Enhancement, relaxation, and reversal of the stereoselectivity for phosphotriesterase by rational evolution of active site residues
    • Chen-Goodspeed, M., Sogorb, M. A., Wu, F. and Raushel, F. M. (2001) Enhancement, relaxation, and reversal of the stereoselectivity for phosphotriesterase by rational evolution of active site residues. Biochemistry 40, 1332-1339
    • (2001) Biochemistry , vol.40 , pp. 1332-1339
    • Chen-Goodspeed, M.1    Sogorb, M.A.2    Wu, F.3    Raushel, F.M.4
  • 39
    • 0035690880 scopus 로고    scopus 로고
    • Zinc coordination sphere in biochemical zinc sites
    • Auld, D. S. (2001) Zinc coordination sphere in biochemical zinc sites. Biometals 14, 271-313
    • (2001) Biometals , vol.14 , pp. 271-313
    • Auld, D.S.1
  • 40
    • 0242500908 scopus 로고    scopus 로고
    • First-second shell interactions in metal binding sites in proteins: A PDB survey and DFT/CDM calculations
    • Dudev, T., Lin, Y. L., Dudev, M. and Lim, C. (2003) First-second shell interactions in metal binding sites in proteins: a PDB survey and DFT/CDM calculations. J. Am. Chem. Soc. 125, 3168-3180
    • (2003) J. Am. Chem. Soc. , vol.125 , pp. 3168-3180
    • Dudev, T.1    Lin, Y.L.2    Dudev, M.3    Lim, C.4
  • 41
    • 0042342591 scopus 로고    scopus 로고
    • Influence of outer-shell metal ligands on the structural and electronic properties of horse liver alcohol dehydrogenase zinc active site
    • Gervasio, F. L., Schettino, V., Mangani, S., Krack, M., Carloni, P. and Parrinello, M. (2003) Influence of outer-shell metal ligands on the structural and electronic properties of horse liver alcohol dehydrogenase zinc active site. J. Phys. Chem. B 107, 6886-6892
    • (2003) J. Phys. Chem. B , vol.107 , pp. 6886-6892
    • Gervasio, F.L.1    Schettino, V.2    Mangani, S.3    Krack, M.4    Carloni, P.5    Parrinello, M.6
  • 42
    • 0035826586 scopus 로고    scopus 로고
    • Thermodynamics of metal ion binding. 2: Metal ion binding by carbonic anhydrase variants
    • DiTusa, C. A., McCall, K. A., Christensen, T., Mahapatro, M., Fierke, C. A. and Toone, E. J. (2001) Thermodynamics of metal ion binding. 2: Metal ion binding by carbonic anhydrase variants. Biochemistry 40, 5345-5351
    • (2001) Biochemistry , vol.40 , pp. 5345-5351
    • DiTusa, C.A.1    McCall, K.A.2    Christensen, T.3    Mahapatro, M.4    Fierke, C.A.5    Toone, E.J.6
  • 43
    • 0028873117 scopus 로고
    • Hydrogen-bond network in the metal-binding site of carbonic-anhydrase enhances zinc affinity and catalytic efficiency
    • Kiefer, L. L., Paterno, S. A. and Fierke, C. A. (1995) Hydrogen-bond network in the metal-binding site of carbonic-anhydrase enhances zinc affinity and catalytic efficiency. J. Am. Chem. Soc. 117, 6831-6837
    • (1995) J. Am. Chem. Soc. , vol.117 , pp. 6831-6837
    • Kiefer, L.L.1    Paterno, S.A.2    Fierke, C.A.3
  • 44
    • 0033200372 scopus 로고    scopus 로고
    • Secondary ligands enhance affinity at a designed metal-binding site
    • Marino, S. F. and Regan, L. (1999) Secondary ligands enhance affinity at a designed metal-binding site. Chem. Biol. 6, 649-655
    • (1999) Chem. Biol. , vol.6 , pp. 649-655
    • Marino, S.F.1    Regan, L.2
  • 45
    • 0031461676 scopus 로고    scopus 로고
    • The extended environment of mononuclear metal centers in protein structures
    • Karlin, S., Zhu, Z. Y. and Karlin, K. D. (1997) The extended environment of mononuclear metal centers in protein structures. Proc. Natl. Acad. Sci. U.S.A. 94, 14225-14230
    • (1997) Proc. Natl. Acad. Sci. U.S.A. , vol.94 , pp. 14225-14230
    • Karlin, S.1    Zhu, Z.Y.2    Karlin, K.D.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.