메뉴 건너뛰기




Volumn 6, Issue 7, 2011, Pages

X-ray structure reveals a new class and provides insight into evolution of alkaline phosphatases

Author keywords

[No Author keywords available]

Indexed keywords

ALKALINE PHOSPHATASE; SERINE;

EID: 79960871721     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0022767     Document Type: Article
Times cited : (17)

References (43)
  • 1
    • 0027456615 scopus 로고
    • Folding and assembly of bacterial alkaline phosphatase in vitro and in vivo
    • Akiyama Y, Ito K, (1993) Folding and assembly of bacterial alkaline phosphatase in vitro and in vivo. J Biol Chem 268: 8146-8150.
    • (1993) J Biol Chem , vol.268 , pp. 8146-8150
    • Akiyama, Y.1    Ito, K.2
  • 2
    • 0025777694 scopus 로고
    • Reaction mechanism of alkaline phosphatase based on crystal structures. Two-metal ion catalysis
    • Kim EE, Wyckoff HW, (1991) Reaction mechanism of alkaline phosphatase based on crystal structures. Two-metal ion catalysis. J Mol Biol 218: 449-464.
    • (1991) J Mol Biol , vol.218 , pp. 449-464
    • Kim, E.E.1    Wyckoff, H.W.2
  • 3
    • 0026773209 scopus 로고
    • Structure and mechanism of alkaline phosphatase
    • Coleman JE, (1992) Structure and mechanism of alkaline phosphatase. Annu Rev Biophys Biomol Struct 21: 441-483.
    • (1992) Annu Rev Biophys Biomol Struct , vol.21 , pp. 441-483
    • Coleman, J.E.1
  • 4
    • 0033605749 scopus 로고    scopus 로고
    • A model of the transition state in the alkaline phosphatase reaction
    • Holtz KM, Stec B, Kantrowitz ER, (1999) A model of the transition state in the alkaline phosphatase reaction. J Biol Chem 274: 8351-8354.
    • (1999) J Biol Chem , vol.274 , pp. 8351-8354
    • Holtz, K.M.1    Stec, B.2    Kantrowitz, E.R.3
  • 5
    • 49549160196 scopus 로고
    • Crystallographic study of alkaline-phosphatase at 7.7 Å resolution
    • Knox JR, Wyckoff HW, (1973) Crystallographic study of alkaline-phosphatase at 7.7 Å resolution. J Mol Biol 74: 533-542.
    • (1973) J Mol Biol , vol.74 , pp. 533-542
    • Knox, J.R.1    Wyckoff, H.W.2
  • 6
    • 0033486058 scopus 로고    scopus 로고
    • Does the active site arginine change the nature of the transition state for alkaline phosphatase-catalyzed phosphoryl transfer?
    • O'Brien PJ, Herschlag D, (1999) Does the active site arginine change the nature of the transition state for alkaline phosphatase-catalyzed phosphoryl transfer? J Am Chem Soc 121: 11022-11023.
    • (1999) J Am Chem Soc , vol.121 , pp. 11022-11023
    • O'Brien, P.J.1    Herschlag, D.2
  • 7
    • 33749333378 scopus 로고    scopus 로고
    • Trapping the tetrahedral intermediate in the alkaline phosphatase reaction by substitution of the active site serine with threonine
    • Wang J, Kantrowitz ER, (2006) Trapping the tetrahedral intermediate in the alkaline phosphatase reaction by substitution of the active site serine with threonine. Protein Sci 15: 2395-2401.
    • (2006) Protein Sci , vol.15 , pp. 2395-2401
    • Wang, J.1    Kantrowitz, E.R.2
  • 8
    • 0035983513 scopus 로고    scopus 로고
    • The 1.9 angstrom crystal structure of heat-labile shrimp alkaline phosphatase
    • de Backer M, McSweeney S, Rasmussen HB, Riise BW, Lindley P, et al. (2002) The 1.9 angstrom crystal structure of heat-labile shrimp alkaline phosphatase. J Mol Biol 318: 1265-1274.
    • (2002) J Mol Biol , vol.318 , pp. 1265-1274
    • de Backer, M.1    McSweeney, S.2    Rasmussen, H.B.3    Riise, B.W.4    Lindley, P.5
  • 9
    • 58149251795 scopus 로고    scopus 로고
    • The 1.4 Å crystal structure of the large and cold-active Vibrio sp. alkaline phosphatase
    • Helland R, Larsen RL, Asgeirsson B, (2009) The 1.4 Å crystal structure of the large and cold-active Vibrio sp. alkaline phosphatase. Biochim Biophys Acta 1794: 297-308.
    • (2009) Biochim Biophys Acta , vol.1794 , pp. 297-308
    • Helland, R.1    Larsen, R.L.2    Asgeirsson, B.3
  • 10
    • 0035937857 scopus 로고    scopus 로고
    • Crystal structure of alkaline phosphatase from human placenta at 1.8 Å resolution - Implication for a substrate specificity
    • Le Du MH, Stigbrand T, Taussig MJ, Menez A, Stura EA, (2001) Crystal structure of alkaline phosphatase from human placenta at 1.8 Å resolution- Implication for a substrate specificity. J Biol Chem 276: 9158-9165.
    • (2001) J Biol Chem , vol.276 , pp. 9158-9165
    • Le du, M.H.1    Stigbrand, T.2    Taussig, M.J.3    Menez, A.4    Stura, E.A.5
  • 11
    • 75649107636 scopus 로고    scopus 로고
    • Crystal structure of cold-active alkaline phosphatase from the psychrophile Shewanella sp
    • Tsuruta H, Mikami B, Higashi T, Aizono Y, (2010) Crystal structure of cold-active alkaline phosphatase from the psychrophile Shewanella sp. Biosci Biotechnol Biochem 74: 69-74.
    • (2010) Biosci Biotechnol Biochem , vol.74 , pp. 69-74
    • Tsuruta, H.1    Mikami, B.2    Higashi, T.3    Aizono, Y.4
  • 12
    • 33846660691 scopus 로고    scopus 로고
    • Crystal structure of alkaline phosphatase from the Antarctic bacterium TAB5
    • Wang E, Koutsioulis D, Leiros HKS, Andersen OA, Bouriotis V, et al. (2007) Crystal structure of alkaline phosphatase from the Antarctic bacterium TAB5. J Mol Biol 366: 1318-1331.
    • (2007) J Mol Biol , vol.366 , pp. 1318-1331
    • Wang, E.1    Koutsioulis, D.2    Leiros, H.K.S.3    Andersen, O.A.4    Bouriotis, V.5
  • 13
    • 0034705337 scopus 로고    scopus 로고
    • A revised mechanism for the alkaline phosphatase reaction involving three metal ions
    • Stec B, Holtz KM, Kantrowitz ER, (2000) A revised mechanism for the alkaline phosphatase reaction involving three metal ions. J Mol Biol 299: 1303-1311.
    • (2000) J Mol Biol , vol.299 , pp. 1303-1311
    • Stec, B.1    Holtz, K.M.2    Kantrowitz, E.R.3
  • 14
    • 47649087237 scopus 로고    scopus 로고
    • Arginine coordination in enzymatic phosphoryl transfer: evaluation of the effect of Arg166 mutations in Escherichia coli alkaline phosphatase
    • O'Brien PJ, Lassila JK, Fenn TD Zalatan JG, Herschlag D, (2008) Arginine coordination in enzymatic phosphoryl transfer: evaluation of the effect of Arg166 mutations in Escherichia coli alkaline phosphatase. Biochemistry 47: 7663-7672.
    • (2008) Biochemistry , vol.47 , pp. 7663-7672
    • O'Brien, P.J.1    Lassila, J.K.2    Fenn TD Zalatan, J.G.3    Herschlag, D.4
  • 15
    • 0032461412 scopus 로고    scopus 로고
    • A superfamily of metalloenzymes unifies phosphopentomutase and cofactor-independent phosphoglycerate mutase with alkaline phosphatases and sulfatases
    • Galperin MY, Bairoch A, Koonin EV, (1998) A superfamily of metalloenzymes unifies phosphopentomutase and cofactor-independent phosphoglycerate mutase with alkaline phosphatases and sulfatases. Protein Sci 7: 1829-1835.
    • (1998) Protein Sci , vol.7 , pp. 1829-1835
    • Galperin, M.Y.1    Bairoch, A.2    Koonin, E.V.3
  • 16
    • 33747517236 scopus 로고    scopus 로고
    • Structural and functional comparisions of nucleotide pyrophosphatase/phosphodiesterase and alkaline phosphatase: implications for mechanism and evolution
    • Zalatan JG, Fenn TD, Brunger AT, Herschlag D, (2006) Structural and functional comparisions of nucleotide pyrophosphatase/phosphodiesterase and alkaline phosphatase: implications for mechanism and evolution. Biochemistry 45: 9788-9803.
    • (2006) Biochemistry , vol.45 , pp. 9788-9803
    • Zalatan, J.G.1    Fenn, T.D.2    Brunger, A.T.3    Herschlag, D.4
  • 17
    • 0033819024 scopus 로고    scopus 로고
    • Structure, function, and evolution of phosphoglycerate mutases: comparision with fructose-2,6-bisphosphatase, acid phosphase, and alkaline phosphatase
    • Jedrzejas MJ, (2000) Structure, function, and evolution of phosphoglycerate mutases: comparision with fructose-2,6-bisphosphatase, acid phosphase, and alkaline phosphatase. Prog Biophys Mol Biol 73: 263-287.
    • (2000) Prog Biophys Mol Biol , vol.73 , pp. 263-287
    • Jedrzejas, M.J.1
  • 18
    • 50949129853 scopus 로고    scopus 로고
    • Cloning and overexpression of alkaline phosphatase SPAP from Sphingomonas sp. strain BSAR-1 for bioprecipitation of uranium from alkaline solutions
    • Nilgiriwala KS, Alahari A, Rao AS, Apte SK, (2008) Cloning and overexpression of alkaline phosphatase SPAP from Sphingomonas sp. strain BSAR-1 for bioprecipitation of uranium from alkaline solutions. Appl Environ Microbiol 74: 5516-5523.
    • (2008) Appl Environ Microbiol , vol.74 , pp. 5516-5523
    • Nilgiriwala, K.S.1    Alahari, A.2    Rao, A.S.3    Apte, S.K.4
  • 19
    • 69849109464 scopus 로고    scopus 로고
    • Crystallization and preliminary X-ray crystallographic analysis of PhoK, an extracellular alkaline phosphatase from Sphingomonas sp BSAR-1
    • Nilgiriwala KS, Bihani SC, Das A, Prashar V, Kumar M, et al. (2009) Crystallization and preliminary X-ray crystallographic analysis of PhoK, an extracellular alkaline phosphatase from Sphingomonas sp BSAR-1. Acta Crystallogr Sect F Struct Biol Cryst Commun 65: 917-919.
    • (2009) Acta Crystallogr Sect F Struct Biol Cryst Commun , vol.65 , pp. 917-919
    • Nilgiriwala, K.S.1    Bihani, S.C.2    Das, A.3    Prashar, V.4    Kumar, M.5
  • 20
    • 0030768043 scopus 로고    scopus 로고
    • Trapping and visualization of a covalent enzyme-phosphate intermediate. Nat Struct Biol
    • Murphy JE, Stec B, Ma L, Kantrowitz ER, (1997) Trapping and visualization of a covalent enzyme-phosphate intermediate. Nat Struct Biol. 4: 618-622.
    • (1997) , vol.4 , pp. 618-622
    • Murphy, J.E.1    Stec, B.2    Ma, L.3    Kantrowitz, E.R.4
  • 21
    • 0036290280 scopus 로고    scopus 로고
    • Artificial evolution of an enzyme active site: structural studies of three highly active mutants of Escherichia coli alkaline phosphatase
    • Le Du MH, Lamoure C, Muller BH, Bulgakov OV, Lajeunesse E, et al. (2002) Artificial evolution of an enzyme active site: structural studies of three highly active mutants of Escherichia coli alkaline phosphatase. J Mol Biol 316: 941-53.
    • (2002) J Mol Biol , vol.316 , pp. 941-953
    • Le du, M.H.1    Lamoure, C.2    Muller, B.H.3    Bulgakov, O.V.4    Lajeunesse, E.5
  • 22
    • 56949087215 scopus 로고    scopus 로고
    • Comparative enzymology in the alkaline phosphatase superfamily to determine the catalytic role of an active site metal ion
    • Zalatan JG, Fenn TD, Herschlag D, (2008) Comparative enzymology in the alkaline phosphatase superfamily to determine the catalytic role of an active site metal ion. J Mol Biol 384: 1174-1189.
    • (2008) J Mol Biol , vol.384 , pp. 1174-1189
    • Zalatan, J.G.1    Fenn, T.D.2    Herschlag, D.3
  • 23
    • 20444390656 scopus 로고    scopus 로고
    • Metal specificity is correlated with two crucial active site residues in Escherichia coli alkaline phosphatase
    • Wang J, Stieglitz KA, Kantrowitz ER, (2005) Metal specificity is correlated with two crucial active site residues in Escherichia coli alkaline phosphatase. Biochemistry 44: 8378-8386.
    • (2005) Biochemistry , vol.44 , pp. 8378-8386
    • Wang, J.1    Stieglitz, K.A.2    Kantrowitz, E.R.3
  • 24
    • 0037184908 scopus 로고    scopus 로고
    • Altering of the metal specificity of Escherichia coli alkaline phosphatase
    • Wojciechowski CL, Kantrowitz ER, (2002) Altering of the metal specificity of Escherichia coli alkaline phosphatase. J Biol Chem 277: 50476-50481.
    • (2002) J Biol Chem , vol.277 , pp. 50476-50481
    • Wojciechowski, C.L.1    Kantrowitz, E.R.2
  • 25
    • 54249149606 scopus 로고    scopus 로고
    • Efficient catalytic promiscuity in an enzyme superfamily: an arylsulfatase shows a rate acceleration of 1013 for phosphate monoester hydrolysis
    • Olguin LF, Askew SE, O'Donoghue AC, Hollfelder F, (2008) Efficient catalytic promiscuity in an enzyme superfamily: an arylsulfatase shows a rate acceleration of 1013 for phosphate monoester hydrolysis. J Am Chem Soc 130: 16547-16555.
    • (2008) J Am Chem Soc , vol.130 , pp. 16547-16555
    • Olguin, L.F.1    Askew, S.E.2    O'Donoghue, A.C.3    Hollfelder, F.4
  • 26
    • 13444307044 scopus 로고    scopus 로고
    • Secondary-structure matching (SSM), a new tool for fast protein structure alignment in three dimensions
    • Krissinel E, Cheng KJ, (2004) Secondary-structure matching (SSM), a new tool for fast protein structure alignment in three dimensions. Acta Crystallogr, Sect D: Biol Crystallogr 60: 2256-2268.
    • (2004) Acta Crystallogr, Sect D: Biol Crystallogr , vol.60 , pp. 2256-2268
    • Krissinel, E.1    Cheng, K.J.2
  • 27
    • 0034599751 scopus 로고    scopus 로고
    • Structure and mechanism of action of a novel phosphoglycerate mutase from Bacillus stearothermophilus
    • Jedrzejas MJ, Chander M, Setlow P, Krishnasamy G, (2000) Structure and mechanism of action of a novel phosphoglycerate mutase from Bacillus stearothermophilus. EMBO J 19: 1419-1431.
    • (2000) EMBO J , vol.19 , pp. 1419-1431
    • Jedrzejas, M.J.1    Chander, M.2    Setlow, P.3    Krishnasamy, G.4
  • 28
    • 77954288774 scopus 로고    scopus 로고
    • Dali server: conservation mapping in 3D
    • Holm L, Rosenström P, (2010) Dali server: conservation mapping in 3D. Nucleic Acids Res 38: 545-549.
    • (2010) Nucleic Acids Res , vol.38 , pp. 545-549
    • Holm, L.1    Rosenström, P.2
  • 31
    • 0027879008 scopus 로고
    • Automatic processing of rotation diffraction data from crystals of initially unknown symmetry and cell constants
    • Kabsch W, (1993) Automatic processing of rotation diffraction data from crystals of initially unknown symmetry and cell constants. J Appl Crystallogr 26: 795-800.
    • (1993) J Appl Crystallogr , vol.26 , pp. 795-800
    • Kabsch, W.1
  • 35
    • 84889120137 scopus 로고
    • Improved methods for building protein models in electron density maps and the location of errors in these models
    • Jones TA, Zou JY, Cowan SW, Kjeldgaard M, (1991) Improved methods for building protein models in electron density maps and the location of errors in these models. Acta Crystallogr A 47: 110-119.
    • (1991) Acta Crystallogr A , vol.47 , pp. 110-119
    • Jones, T.A.1    Zou, J.Y.2    Cowan, S.W.3    Kjeldgaard, M.4
  • 36
    • 33646260450 scopus 로고    scopus 로고
    • Optimal description of a protein structure in terms of multiple groups undergoing TLS motion
    • Painter J, Merritt EA, (2006) Optimal description of a protein structure in terms of multiple groups undergoing TLS motion. Acta Crystallogr, Sect D: Biol Crystallogr 62: 439-450.
    • (2006) Acta Crystallogr, Sect D: Biol Crystallogr , vol.62 , pp. 439-450
    • Painter, J.1    Merritt, E.A.2
  • 37
    • 33645158291 scopus 로고    scopus 로고
    • TLSMD web server for the generation of multi-group TLS models
    • Painter J, Merritt EA, (2006) TLSMD web server for the generation of multi-group TLS models. J Appl Crystallogr 19: 109-111.
    • (2006) J Appl Crystallogr , vol.19 , pp. 109-111
    • Painter, J.1    Merritt, E.A.2
  • 39
    • 0043123208 scopus 로고    scopus 로고
    • ESPript/ENDscript: extracting and rendering sequence and 3D information from atomic structures of proteins. Nucl
    • Gouet P, Robert X, Courcelle E, (2003) ESPript/ENDscript: extracting and rendering sequence and 3D information from atomic structures of proteins. Nucl. Acids Res 31: 3320-3323.
    • (2003) Acids Res , vol.31 , pp. 3320-3323
    • Gouet, P.1    Robert, X.2    Courcelle, E.3
  • 40
    • 34548232365 scopus 로고    scopus 로고
    • Inference of macromolecular assemblies from crystalline state
    • Krissinel E, Henrick K, (2007) Inference of macromolecular assemblies from crystalline state. J Mol Biol 372: 774-797.
    • (2007) J Mol Biol , vol.372 , pp. 774-797
    • Krissinel, E.1    Henrick, K.2
  • 42
    • 33749442647 scopus 로고    scopus 로고
    • MultiSeq: unifying sequence and structure data for evolutionary Analysis
    • Roberts E, Eargle J, Wright D, Luthey-Schulten Z, (2006) MultiSeq: unifying sequence and structure data for evolutionary Analysis. BMC Bioinformatics 7: 382-392.
    • (2006) BMC Bioinformatics , vol.7 , pp. 382-392
    • Roberts, E.1    Eargle, J.2    Wright, D.3    Luthey-Schulten, Z.4
  • 43
    • 0346848759 scopus 로고    scopus 로고
    • On the evolution of structure in aminoacyl-tRNA synthetases
    • O'Donoghue P, Luthey-Schulten Z, (2003) On the evolution of structure in aminoacyl-tRNA synthetases. Microbiol Mol Biol Rev 67: 550-573.
    • (2003) Microbiol Mol Biol Rev , vol.67 , pp. 550-573
    • O'Donoghue, P.1    Luthey-Schulten, Z.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.