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Volumn 291, Issue 1, 1999, Pages 135-147

Three-dimensional structure of a mammalian purple acid phosphatase at 2.2 Å resolution with a μ-(hydr)oxo bridged di-iron center

Author keywords

Bone resorption; Di iron center; Enzyme mechanism; Phosphatase; Protein crystallography

Indexed keywords

ACID PHOSPHATASE; IRON; VEGETABLE PROTEIN;

EID: 0345151820     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.1999.2962     Document Type: Article
Times cited : (127)

References (60)
  • 1
    • 0022634536 scopus 로고
    • Immunocytochemical localisation of a tartrate resistant and vanadate-sensitive acid nucleotide tri- And diphosphatase
    • Andersson G. N., Ek-Rylander B., Hammarström L. E., Lindskog S., Toverud S. U. Immunocytochemical localisation of a tartrate resistant and vanadate-sensitive acid nucleotide tri- and diphosphatase. J. Histochem. Cytochem. 34:1986;293-298.
    • (1986) J. Histochem. Cytochem. , vol.34 , pp. 293-298
    • Andersson, G.N.1    Ek-Rylander, B.2    Hammarström, L.E.3    Lindskog, S.4    Toverud, S.U.5
  • 3
    • 0020490694 scopus 로고
    • Detection of a g′=1. 74 EPR signal in bovine spleen purple acid phosphatase
    • Antanaitis B. C., Aisen P. Detection of a g′=1. 74 EPR signal in bovine spleen purple acid phosphatase. J. Biol. Chem. 257:1982;5330-5332.
    • (1982) J. Biol. Chem. , vol.257 , pp. 5330-5332
    • Antanaitis, B.C.1    Aisen, P.2
  • 4
    • 0021099223 scopus 로고
    • Physical characterization of two-iron uteroferrin. Magnetic interactions and active-site structure
    • Antanaitis B. C., Aisen P., Lilienthal H. R. Physical characterization of two-iron uteroferrin. Magnetic interactions and active-site structure. J. Biol. Chem. 258:1983;3166-3172.
    • (1983) J. Biol. Chem. , vol.258 , pp. 3166-3172
    • Antanaitis, B.C.1    Aisen, P.2    Lilienthal, H.R.3
  • 5
    • 37049073676 scopus 로고
    • Mechanism of the reaction of different phosphates with the iron(II)iron(III) form of purple acid phosphatase from porcine uteri
    • Aquino M. A. S., Lim J.-S., Sykes A. G. Mechanism of the reaction of different phosphates with the iron(II)iron(III) form of purple acid phosphatase from porcine uteri. J. Chem. Soc. Dalton Trans. 1994;429-436.
    • (1994) J. Chem. Soc. Dalton Trans. , pp. 429-436
    • Aquino, M.A.S.1    Lim, J.-S.2    Sykes, A.G.3
  • 8
    • 0028800913 scopus 로고
    • Generation and characterization of monoclonal antibodies to human type-5 tartrate resistant acid phosphatase: Development of specific immunoassay of the isoenzyme in serum
    • Chamberlain P., Compston J., Cox T. M., Hayman A. R., Imrie R. C., Reynolds K., Holmes S. D. Generation and characterization of monoclonal antibodies to human type-5 tartrate resistant acid phosphatase: development of specific immunoassay of the isoenzyme in serum. Clin. Chem. 41:1995;1495-1499.
    • (1995) Clin. Chem. , vol.41 , pp. 1495-1499
    • Chamberlain, P.1    Compston, J.2    Cox, T.M.3    Hayman, A.R.4    Imrie, R.C.5    Reynolds, K.6    Holmes, S.D.7
  • 11
    • 0025162350 scopus 로고
    • Anion binding to uteroferrin. Evidence for phosphate coordination to the iron(III) ion of the dinuclear active-site and interaction with the hydroxo bridge
    • David S. S., Que L. Jr. Anion binding to uteroferrin. Evidence for phosphate coordination to the iron(III) ion of the dinuclear active-site and interaction with the hydroxo bridge. J. Am. Chem. Soc. 112:1990;6455-6463.
    • (1990) J. Am. Chem. Soc. , vol.112 , pp. 6455-6463
    • David, S.S.1    Que L., Jr.2
  • 12
    • 0025294506 scopus 로고
    • Peptide sequences that target cytosolic proteins for lysosomal proteolysis
    • Dice J. F. Peptide sequences that target cytosolic proteins for lysosomal proteolysis. Trends Biochem. Sci. 15:1990;305-309.
    • (1990) Trends Biochem. Sci. , vol.15 , pp. 305-309
    • Dice, J.F.1
  • 13
    • 0025909426 scopus 로고
    • Purple acid phosphatase from bovine spleen. Interactions at the active-site in relation to the reaction mechanism
    • Dietrich M., Münstermann D., Suerbaum H., Witzel H. Purple acid phosphatase from bovine spleen. Interactions at the active-site in relation to the reaction mechanism. Eur. J. Biochem. 199:1991;105-113.
    • (1991) Eur. J. Biochem. , vol.199 , pp. 105-113
    • Dietrich, M.1    Münstermann, D.2    Suerbaum, H.3    Witzel, H.4
  • 14
    • 0002272476 scopus 로고
    • The binuclear iron centers of uteroferrin and the purple acid phosphatases
    • Doi K., Antanaitis B. C., Aisen P. The binuclear iron centers of uteroferrin and the purple acid phosphatases. Struct. Bonding. 70:1988;1-26.
    • (1988) Struct. Bonding , vol.70 , pp. 1-26
    • Doi, K.1    Antanaitis, B.C.2    Aisen, P.3
  • 15
    • 0026340595 scopus 로고
    • Cloning, sequence, and developmental expression of a type 5, tatrate resistant, acid phosphatase of rat bone
    • Ek-Rylander B., Bill P., Norgård M., Nilsson S., Andersson G. Cloning, sequence, and developmental expression of a type 5, tatrate resistant, acid phosphatase of rat bone. J. Biol. Chem. 266:1991a;24684-24689.
    • (1991) J. Biol. Chem. , vol.266 , pp. 24684-24689
    • Ek-Rylander, B.1    Bill, P.2    Norgård, M.3    Nilsson, S.4    Andersson, G.5
  • 16
    • 0025811727 scopus 로고
    • Characterization of a tartrate-resistant acid phosphatase (ATPase) from rat bone: Hydrodynamic properties and N-terminal amino acid sequence
    • Ek-Rylander B., Bergman T., Andersson G. Characterization of a tartrate-resistant acid phosphatase (ATPase) from rat bone: hydrodynamic properties and N-terminal amino acid sequence. J. Bone Miner. Res. 6:1991b;365-373.
    • (1991) J. Bone Miner. Res. , vol.6 , pp. 365-373
    • Ek-Rylander, B.1    Bergman, T.2    Andersson, G.3
  • 17
    • 0028237439 scopus 로고
    • Dephosphorylation of osteopontin and bone sialoprotein by osteoclastic tartrate-resistant acid phosphatase. Modulation of osteoclast adhesion in vitro
    • Ek-Rylander B., Flores M., Wendel M., Heinegård D., Andersson G. Dephosphorylation of osteopontin and bone sialoprotein by osteoclastic tartrate-resistant acid phosphatase. Modulation of osteoclast adhesion in vitro. J. Biol. Chem. 269:1994;14853-14856.
    • (1994) J. Biol. Chem. , vol.269 , pp. 14853-14856
    • Ek-Rylander, B.1    Flores, M.2    Wendel, M.3    Heinegård, D.4    Andersson, G.5
  • 18
    • 0031036061 scopus 로고    scopus 로고
    • Comparative studies of rat recombinant purple acid phosphatase and bone tartrate-resistant acid phosphatase
    • Ek-Rylander B., Barkhem T., Ljusberg J., Öhman L., Andersson K. K., Andersson G. Comparative studies of rat recombinant purple acid phosphatase and bone tartrate-resistant acid phosphatase. Biochem. J. 321:1997;305-311.
    • (1997) Biochem. J. , vol.321 , pp. 305-311
    • Ek-Rylander, B.1    Barkhem, T.2    Ljusberg, J.3    Öhman, L.4    Andersson, K.K.5    Andersson, G.6
  • 19
    • 0018787258 scopus 로고
    • Resonance Raman scattering from uteroferrin, the purple glycoprotein of the porcine uterus
    • Gaber B. P., Sheridan J. P., Bazer F. W., Roberts R. M. Resonance Raman scattering from uteroferrin, the purple glycoprotein of the porcine uterus. J. Biol. Chem. 254:1979;8340-8342.
    • (1979) J. Biol. Chem. , vol.254 , pp. 8340-8342
    • Gaber, B.P.1    Sheridan, J.P.2    Bazer, F.W.3    Roberts, R.M.4
  • 20
    • 0029094754 scopus 로고
    • Three-dimensional structure of the catalytic subunit of protein serine/threonine phosphatase-1
    • Goldberg J., Huang H.-B., Kwon Y.-G., Greengard P., Nairn A. C., Kuriyan J. Three-dimensional structure of the catalytic subunit of protein serine/threonine phosphatase-1. Nature. 376:1995;745-753.
    • (1995) Nature , vol.376 , pp. 745-753
    • Goldberg, J.1    Huang, H.-B.2    Kwon, Y.-G.3    Greengard, P.4    Nairn, A.C.5    Kuriyan, J.6
  • 22
    • 0029759431 scopus 로고    scopus 로고
    • Tartrate-resistant acid phosphatase from human bone: Purification and development of an immunoassay
    • Halleen J., Hentunen T. A., Hellman J., Väänänen H. K. Tartrate-resistant acid phosphatase from human bone: purification and development of an immunoassay. J. Bone Miner. Res. 11:1996;1444-1452.
    • (1996) J. Bone Miner. Res. , vol.11 , pp. 1444-1452
    • Halleen, J.1    Hentunen, T.A.2    Hellman, J.3    Väänänen, H.K.4
  • 23
    • 0032053256 scopus 로고    scopus 로고
    • Studies on the protein tyrosine phosphatase activity of tartrate-resistant acid phosphatase
    • Halleen J., Kaija H., Stepan J. J., Vihko P., Väänänen H. K. Studies on the protein tyrosine phosphatase activity of tartrate-resistant acid phosphatase. Arch. Biochem. Biophys. 352:1998;97-102.
    • (1998) Arch. Biochem. Biophys. , vol.352 , pp. 97-102
    • Halleen, J.1    Kaija, H.2    Stepan, J.J.3    Vihko, P.4    Väänänen, H.K.5
  • 24
    • 0028009805 scopus 로고
    • Purple acid phosphatase of the human macrophage and osteoclast
    • Hayman A. R., Cox T. M. Purple acid phosphatase of the human macrophage and osteoclast. J. Biol. Chem. 269:1994;1294-1300.
    • (1994) J. Biol. Chem. , vol.269 , pp. 1294-1300
    • Hayman, A.R.1    Cox, T.M.2
  • 25
    • 0029851956 scopus 로고    scopus 로고
    • Mice lacking tartrate-resistant acid phosphatase (Acp 5) have disrupted endochondral ossification and mild osteopetrosis
    • Hayman A. R., Jones S. J., Boyde A., Foster D., Colledge W. H., Carlton M. B., Evans M. J., Cox T. M. Mice lacking tartrate-resistant acid phosphatase (Acp 5) have disrupted endochondral ossification and mild osteopetrosis. Development. 122:1996;3151-3162.
    • (1996) Development , vol.122 , pp. 3151-3162
    • Hayman, A.R.1    Jones, S.J.2    Boyde, A.3    Foster, D.4    Colledge, W.H.5    Carlton, M.B.6    Evans, M.J.7    Cox, T.M.8
  • 26
    • 0000282384 scopus 로고
    • NOESY studies on the FeIIICoII active-site of the purple acid phosphatase uteroferrin
    • Holz R. C., Que L. Jr, Ming J.-L. NOESY studies on the FeIIICoII active-site of the purple acid phosphatase uteroferrin. J. Am. Chem. Soc. 114:1992;4434-4436.
    • (1992) J. Am. Chem. Soc. , vol.114 , pp. 4434-4436
    • Holz, R.C.1    Que L., Jr.2    Ming, J.-L.3
  • 27
    • 84889120137 scopus 로고
    • Improved methods for building protein models in electron density maps and location of errors in these maps
    • Jones T. A., Zou J.-Y., Cowan S., Kjeldgaard M. Improved methods for building protein models in electron density maps and location of errors in these maps. Acta Crystallog. sect. A. 47:1991;100-119.
    • (1991) Acta Crystallog. Sect. a , vol.47 , pp. 100-119
    • Jones, T.A.1    Zou, J.-Y.2    Cowan, S.3    Kjeldgaard, M.4
  • 28
    • 0033014135 scopus 로고    scopus 로고
    • Tartrate-resistant acid phosphatase: Large scale production and purification of the recombinant enzyme, characterization and crystallization
    • Kaija H., Jia J., Lindqvist Y., Andersson G. N., Vihko P. T. Tartrate-resistant acid phosphatase: large scale production and purification of the recombinant enzyme, characterization and crystallization. J. Bone Miner. Res. 14:1999;424-430.
    • (1999) J. Bone Miner. Res. , vol.14 , pp. 424-430
    • Kaija, H.1    Jia, J.2    Lindqvist, Y.3    Andersson, G.N.4    Vihko, P.T.5
  • 30
    • 0030596529 scopus 로고    scopus 로고
    • Mechanism of Fe(III)-Zn(II) purple acid phosphatase based on crystal structures
    • Klabunde T., Sträter N., Fröhlich R., Witzel H., Krebs B. Mechanism of Fe(III)-Zn(II) purple acid phosphatase based on crystal structures. J. Mol. Biol. 259:1996;737-748.
    • (1996) J. Mol. Biol. , vol.259 , pp. 737-748
    • Klabunde, T.1    Sträter, N.2    Fröhlich, R.3    Witzel, H.4    Krebs, B.5
  • 32
    • 0030497978 scopus 로고    scopus 로고
    • Efficient rebuilding of protein structures
    • Kleywegt G. J., Jones T. A. Efficient rebuilding of protein structures. Acta Crystallog. sect. D. 52:1996;829-832.
    • (1996) Acta Crystallog. Sect. D , vol.52 , pp. 829-832
    • Kleywegt, G.J.1    Jones, T.A.2
  • 33
    • 0028268627 scopus 로고
    • Conserved sequence pattern in a wide variety of phosphoesterases
    • Koonin E. V. Conserved sequence pattern in a wide variety of phosphoesterases. Protein Sci. 3:1994;356-358.
    • (1994) Protein Sci. , vol.3 , pp. 356-358
    • Koonin, E.V.1
  • 34
    • 0026244229 scopus 로고
    • MOLSCIPT: A program to produce both detailed and schematic plots of protein structure
    • Kraulis P. MOLSCIPT: a program to produce both detailed and schematic plots of protein structure. J. Appl. Crystallog. 24:1991;946-950.
    • (1991) J. Appl. Crystallog. , vol.24 , pp. 946-950
    • Kraulis, P.1
  • 36
    • 0023103333 scopus 로고
    • Purification and characterization of an acid phosphatase that displays phosphotyrosyl-protein phosphatase acticity from bovine cortical bone matrix
    • Lau K.-H. W., Freeman T., Baylink D. J. Purification and characterization of an acid phosphatase that displays phosphotyrosyl-protein phosphatase acticity from bovine cortical bone matrix. J. Biol. Chem. 262:1987;1389-1397.
    • (1987) J. Biol. Chem. , vol.262 , pp. 1389-1397
    • Lau, K.-H.W.1    Freeman, T.2    Baylink, D.J.3
  • 38
    • 0003115798 scopus 로고    scopus 로고
    • A www service system for automatic comparison of protein structures
    • Lu G. A www service system for automatic comparison of protein structures. Protein Data Bank Quart. Newsletter. 78:1996;10-11.
    • (1996) Protein Data Bank Quart. Newsletter , vol.78 , pp. 10-11
    • Lu, G.1
  • 40
    • 0028057108 scopus 로고
    • Raster 3D version 2.0: A program for photorealistic molecular graphics
    • Merrit E. A., Murphy M. E. P. Raster 3D version 2.0: a program for photorealistic molecular graphics. Acta Crystallog. sect. D. 50:1994;869-873.
    • (1994) Acta Crystallog. Sect. D , vol.50 , pp. 869-873
    • Merrit, E.A.1    Murphy, M.E.P.2
  • 41
    • 85021609916 scopus 로고
    • Purple acid phosphatase: A diiron enzyme that catalyzes a direct phospho-group transfer to water
    • Mueller E. G., Crowder M. W., Averill B. A., Knowles J. R. Purple acid phosphatase: a diiron enzyme that catalyzes a direct phospho-group transfer to water. J. Am. Chem. Soc. 115:1993;2974-2975.
    • (1993) J. Am. Chem. Soc. , vol.115 , pp. 2974-2975
    • Mueller, E.G.1    Crowder, M.W.2    Averill, B.A.3    Knowles, J.R.4
  • 42
    • 0030924992 scopus 로고    scopus 로고
    • Refinement of macromolecular structures by the maximum-likelihood method
    • Murshudov G. N., Vagin A. A., Dodson E. J. Refinement of macromolecular structures by the maximum-likelihood method. Acta Crystallog. sect. D. 53:1997;240-253.
    • (1997) Acta Crystallog. Sect. D , vol.53 , pp. 240-253
    • Murshudov, G.N.1    Vagin, A.A.2    Dodson, E.J.3
  • 43
    • 84920325457 scopus 로고
    • AMoRe: An automated package for molecular replacement
    • Navaza J. AMoRe: an automated package for molecular replacement. Acta Crystallog. sect. A. 50:1994;157-163.
    • (1994) Acta Crystallog. Sect. a , vol.50 , pp. 157-163
    • Navaza, J.1
  • 44
    • 0026319199 scopus 로고
    • Protein folding and association: Insights from the interfacial and thermodynamic properties of hydrocarbons
    • Nicholls A., Sharp K. A., Honig B. Protein folding and association: insights from the interfacial and thermodynamic properties of hydrocarbons. Proteins: Struct. Funct. Genet. 11:1991;281-296.
    • (1991) Proteins: Struct. Funct. Genet. , vol.11 , pp. 281-296
    • Nicholls, A.1    Sharp, K.A.2    Honig, B.3
  • 46
    • 0027340545 scopus 로고
    • Asp304 of Escherichia coli acid phosphatase is involved in leaving group protonation
    • Ostanin K., van Etten R. L. Asp304 of Escherichia coli acid phosphatase is involved in leaving group protonation. J. Biol. Chem. 268:1993;20778-20784.
    • (1993) J. Biol. Chem. , vol.268 , pp. 20778-20784
    • Ostanin, K.1    Van Etten, R.L.2
  • 47
    • 0027283994 scopus 로고
    • Purification and properties of the native form of the purple acid phosphatase from bovine spleen
    • Orlando J. L., Zirino T., Quirk B. J., Averill B. A. Purification and properties of the native form of the purple acid phosphatase from bovine spleen. Biochemistry. 32:1993;8120-8129.
    • (1993) Biochemistry , vol.32 , pp. 8120-8129
    • Orlando, J.L.1    Zirino, T.2    Quirk, B.J.3    Averill, B.A.4
  • 49
    • 84944812409 scopus 로고
    • Improved coefficients for map calculation using partial structures with errors
    • Read R. J. Improved coefficients for map calculation using partial structures with errors. Acta Crystallog. sect. A. 42:1986;140-149.
    • (1986) Acta Crystallog. Sect. a , vol.42 , pp. 140-149
    • Read, R.J.1
  • 50
    • 0019443447 scopus 로고
    • The anatomy and taxonomy of protein structure
    • Richardson J. The anatomy and taxonomy of protein structure. Advan. Protein Chem. 34:1981;167-330.
    • (1981) Advan. Protein Chem. , vol.34 , pp. 167-330
    • Richardson, J.1
  • 52
    • 0025285237 scopus 로고
    • NMR studies of the dinuclear iron site in reduced uteroferrin and its oxoanion complexes
    • Scarrow R. C., Pyrz J. W., Que L. Jr. NMR studies of the dinuclear iron site in reduced uteroferrin and its oxoanion complexes. J. Am. Chem. Soc. 112:1990;657-665.
    • (1990) J. Am. Chem. Soc. , vol.112 , pp. 657-665
    • Scarrow, R.C.1    Pyrz, J.W.2    Que L., Jr.3
  • 53
    • 0029640070 scopus 로고
    • Crystal structure of a purple acid phosphatase containg a dinuclear Fe(III)-Zn(II) active-site
    • Sträter N., Klabunde T., Tucker P., Witzel H., Krebs B. Crystal structure of a purple acid phosphatase containg a dinuclear Fe(III)-Zn(II) active-site. Science. 268:1995;1489-1492.
    • (1995) Science , vol.268 , pp. 1489-1492
    • Sträter, N.1    Klabunde, T.2    Tucker, P.3    Witzel, H.4    Krebs, B.5
  • 55
    • 0025222988 scopus 로고
    • An enzyme with a double identity: Purple acid phosphatase and tartrate resistant acid phosphatase
    • Vincent J. B., Averill B. A. An enzyme with a double identity: purple acid phosphatase and tartrate resistant acid phosphatase. FASEB J. 4:1990;3009-3014.
    • (1990) FASEB J. , vol.4 , pp. 3009-3014
    • Vincent, J.B.1    Averill, B.A.2
  • 56
    • 0026075511 scopus 로고
    • Evidence for a phosphoryl-enzyme intermediate in phosphate ester hydrolysis by purple acid phosphatase from bovine spleen
    • Vincent J. B., Crowder M. W., Averill B. A. Evidence for a phosphoryl-enzyme intermediate in phosphate ester hydrolysis by purple acid phosphatase from bovine spleen. J. Biol. Chem. 266:1991;17737-17740.
    • (1991) J. Biol. Chem. , vol.266 , pp. 17737-17740
    • Vincent, J.B.1    Crowder, M.W.2    Averill, B.A.3
  • 57
    • 0026535321 scopus 로고
    • Hydrolysis of phosphate monoesters: A biological problem with multiple chemical solutions
    • Vincent J. B., Crowder M. W., Averill B. A. Hydrolysis of phosphate monoesters: a biological problem with multiple chemical solutions. Trends in Biochem. Sci. 17:1992;105-110.
    • (1992) Trends in Biochem. Sci. , vol.17 , pp. 105-110
    • Vincent, J.B.1    Crowder, M.W.2    Averill, B.A.3
  • 58
    • 0032568594 scopus 로고    scopus 로고
    • Extended X-ray absorption fine structure studies of the anion complexes of FeZn uteroferrin
    • Wang X., Que L. Jr. Extended X-ray absorption fine structure studies of the anion complexes of FeZn uteroferrin. Biochemistry. 37:1998;7813-7821.
    • (1998) Biochemistry , vol.37 , pp. 7813-7821
    • Wang, X.1    Que L., Jr.2
  • 59
    • 0026610832 scopus 로고
    • 1H NMR and NOE studies of the purple acid phosphatase from porcine uterus and bovine spleen
    • Wang Z., Ming L. J., Que L. Jr, Vincent J. B., Crowder M. W., Averill B. A. 1H NMR and NOE studies of the purple acid phosphatase from porcine uterus and bovine spleen. Biochemistry. 31:1992;5263-5268.
    • (1992) Biochemistry , vol.31 , pp. 5263-5268
    • Wang, Z.1    Ming, L.J.2    Que L., Jr.3    Vincent, J.B.4    Crowder, M.W.5    Averill, B.A.6


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