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Volumn 7, Issue 2, 2000, Pages 147-153

Crystal structures of a novel, thermostable phytase in partially and fully calcium-loaded states

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACID; CALCIUM; INOSITOL DERIVATIVE; PHOSPHATE; PHYTASE; PHYTATE; PHYTIC ACID;

EID: 0033950597     PISSN: 10728368     EISSN: None     Source Type: Journal    
DOI: 10.1038/72421     Document Type: Article
Times cited : (131)

References (36)
  • 2
    • 0006135911 scopus 로고
    • Biological availability of phosphorus for pigs
    • Common, F.H. Biological availability of phosphorus for pigs. Nature 143,370-380 (1989).
    • (1989) Nature , vol.143 , pp. 370-380
    • Common, F.H.1
  • 6
    • 0030684148 scopus 로고    scopus 로고
    • Molecular cloning and expression of a rat hepatic multiple inositol polyphosphate phosphatase
    • Craxton, A., Caffrey, 1.1., Burkhart, W., Safrany, S.T. & Shears, S.B. Molecular cloning and expression of a rat hepatic multiple inositol polyphosphate phosphatase. Biochem. J. 328,75-81 (1997).
    • (1997) Biochem. J. , vol.328 , pp. 75-81
    • Craxton, A.1    Caffrey, I.I.2    Burkhart, W.3    Safrany, S.T.4    Shears, S.B.5
  • 7
    • 0025787109 scopus 로고
    • Cyclohexanedione modification of arginine at the active site of Aspergillus ficuum phytase
    • Ullah, A.M., Cummins, B.J.& Dischinger, H.C. Cyclohexanedione modification of arginine at the active site of Aspergillus ficuum phytase. Biochem. Biophys. Res. Commun. 178, 45-53 (1991).
    • (1991) Biochem. Biophys. Res. Commun. , vol.178 , pp. 45-53
    • Ullah, A.M.1    Cummins, B.J.2    Dischinger, H.C.3
  • 8
    • 0031039664 scopus 로고    scopus 로고
    • Crystal structure of phytase from Aspergillus ficuum at 2.5 Å resolution
    • Kostrewa, D. et al. Crystal structure of phytase from Aspergillus ficuum at 2.5 Å resolution. Nature Struct. Biol. 4,185-190 (1997).
    • (1997) Nature Struct. Biol. , vol.4 , pp. 185-190
    • Kostrewa, D.1
  • 9
    • 0026493674 scopus 로고
    • Structure of inositol monophosphatase, the putative target of lithium therapy
    • Bone, R., Springer, J.P.& Atack, J.R. Structure of inositol monophosphatase, the putative target of lithium therapy. Proc. Wat/. Acad. Sei. USA 89, 10031-10035 (1992).
    • (1992) Proc. Wat/. Acad. Sei. USA , vol.89 , pp. 10031-10035
    • Bone, R.1    Springer, J.P.2    Atack, J.R.3
  • 10
    • 0028109640 scopus 로고
    • Crystal structure of inositol polyphosphate 1-phosphatase at 2.3 Å resolution
    • York, J.D., Ponder, J.W.. Chen. Z., Mathews, F.S. & Majerus, P.W. Crystal structure of inositol polyphosphate 1-phosphatase at 2.3 Å resolution. Biochemistry 33, 13164-13171 (1994).
    • (1994) Biochemistry , vol.33 , pp. 13164-13171
    • York, J.D.1    Ponder, J.W.2    Chen, Z.3    Mathews, F.S.4    Majerus, P.W.5
  • 13
    • 0032080595 scopus 로고    scopus 로고
    • Cloning of the thermostable phytase gene (phy) from Bacillus sp. DS11 and its overexpression in Escherichia coll
    • Kirn. Y.O., Lee. J.K., Kim, H.K., Yu, J.H.& Oh. T.K. Cloning of the thermostable phytase gene (phy) from Bacillus sp. DS11 and its overexpression in Escherichia coll. FEMS Microbiol. Lett. 162,185-191 (1998).
    • (1998) FEMS Microbiol. Lett. , vol.162 , pp. 185-191
    • Kirn, Y.O.1    Lee, J.K.2    Kim, H.K.3    Yu, J.H.4    Oh, T.K.5
  • 14
    • 0031982859 scopus 로고    scopus 로고
    • Purification and properties of a thermostable phytase from Bacillus sp. DS11
    • Kim, Y.O., Kim, H.K., Bae, K.-S., Yu, J.H.& Oh, T.K. Purification and properties of a thermostable phytase from Bacillus sp. DS11. Enzyme and Microbial Technot. 22, 2-7(1998).
    • (1998) Enzyme and Microbial Technot. , vol.22 , pp. 2-7
    • Kim, Y.O.1    Kim, H.K.2    Bae, K.-S.3    Yu, J.H.4    Oh, T.K.5
  • 16
    • 0027440362 scopus 로고
    • Protein structure comparison by alignment of distance matrices
    • Holm, L.& Sanders, C. Protein structure comparison by alignment of distance matrices. J. Mol. Biol. 223,123-138 (1993).
    • (1993) J. Mol. Biol. , vol.223 , pp. 123-138
    • Holm, L.1    Sanders, C.2
  • 17
    • 0020629047 scopus 로고
    • Structure of the influenza virus glycoprotein antigen neuraminidase at 2.9 Å resolution
    • Varghese, J.N., Laver, W.G.& Colman, P.M. Structure of the influenza virus glycoprotein antigen neuraminidase at 2.9 Å resolution. Nature 303, 35-40 (1983).
    • (1983) Nature , vol.303 , pp. 35-40
    • Varghese, J.N.1    Laver, W.G.2    Colman, P.M.3
  • 18
    • 0033522648 scopus 로고    scopus 로고
    • The 1.7 Å crystal structure of the apo form of the soluble quinoprotein glucose dehydrogenase from Acnetobacter ca/coacet/cus reveals a novel internal conserved sequence repeat
    • Oubrie, A., Rozeboom, HJ., Kalk, K.H., Duine, J.A.& Dijkstra, B.W. The 1.7 Å crystal structure of the apo form of the soluble quinoprotein glucose dehydrogenase from Acnetobacter ca/coacet/cus reveals a novel internal conserved sequence repeat. J. Mol. Biol. 289,319-333 (1999).
    • (1999) J. Mol. Biol. , vol.289 , pp. 319-333
    • Oubrie, A.1    Rozeboom, H.J.2    Kalk, K.H.3    Duine, J.A.4    Dijkstra, B.W.5
  • 19
    • 0032485075 scopus 로고    scopus 로고
    • The 1.7 Å crystal structure of the regulator of chromosome condensation (RCC1) reveals a seven-bladed propeller
    • Renault, L. et a/. The 1.7 Å crystal structure of the regulator of chromosome condensation (RCC1) reveals a seven-bladed propeller. Nature 392, 97-101 (1998).
    • (1998) Nature , vol.392 , pp. 97-101
    • Renault, L.1
  • 20
    • 1842412487 scopus 로고    scopus 로고
    • Haem-ligand switching during catalysis in crystals of a nitrogen-cycle enzyme
    • Williams, P.A. et al. Haem-ligand switching during catalysis in crystals of a nitrogen-cycle enzyme. Nature 389,406-412 (1997).
    • (1997) Nature , vol.389 , pp. 406-412
    • Williams, P.A.1
  • 21
    • 0029593456 scopus 로고
    • 2
    • 2. Cell 83, 1047-1058(1995).
    • (1995) Cell , vol.83 , pp. 1047-1058
    • Wall, M.A.1
  • 22
    • 0029664589 scopus 로고    scopus 로고
    • The 2.0 Å crystal structure of a heterotrimeric G protein
    • Lambright, D.G. et a/. The 2.0 Å crystal structure of a heterotrimeric G protein. Nature 379, 311-319(1996).
    • (1996) Nature , vol.379 , pp. 311-319
    • Lambright, D.G.1
  • 23
    • 13044293392 scopus 로고    scopus 로고
    • Preliminary x-ray crystallographic analysis of a novel phytase from a Bacillus amyloliquefaciens strain
    • Ha, N.-C, Kirn, Y.-O, Oh, T.-K.& Oh, B.-H. Preliminary x-ray crystallographic analysis of a novel phytase from a Bacillus amyloliquefaciens strain. Acta Crystallogr. D 55, 691-693 (1999).
    • (1999) Acta Crystallogr. D , vol.55 , pp. 691-693
    • Ha, N.-C.1    Kirn, Y.-O.2    Oh, T.-K.3    Oh, B.-H.4
  • 24
    • 0028894334 scopus 로고
    • Calcium and membrane binding properties of bovine neurocalcin 6 expressed in
    • Ladent, D. Calcium and membrane binding properties of bovine neurocalcin 6 expressed in Escherkhia coli. J. Biol. Chem. 270, 3179-3185 (1995).
    • (1995) Escherkhia Coli. J. Biol. Chem. , vol.270 , pp. 3179-3185
    • Ladent, D.1
  • 25
    • 0023771079 scopus 로고
    • Refined crystal structure of troponin C from turkey skeletal muscle at 2.0 Å resolution
    • Herzberg, O.& James, M.N. Refined crystal structure of troponin C from turkey skeletal muscle at 2.0 Å resolution. J. Mol .Biol. 203, 761-779 (1988).
    • (1988) J. Mol .Biol. , vol.203 , pp. 761-779
    • Herzberg, O.1    James, M.N.2
  • 26
    • 13144305048 scopus 로고    scopus 로고
    • Activation of Bacillus licheniformis α-amylase through a disorder → order transition of the substratebinding site mediated by a calcium-sodium-calcium metal triad
    • Machius, M., Declerck, N., Huber. R.& Wiegand, G. Activation of Bacillus licheniformis α-amylase through a disorder → order transition of the substratebinding site mediated by a calcium-sodium-calcium metal triad. Structure 6, 281-292(1998).
    • (1998) Structure , vol.6 , pp. 281-292
    • Machius, M.1    Declerck, N.2    Huber, R.3    Wiegand, G.4
  • 27
    • 0029932580 scopus 로고    scopus 로고
    • Analysis of protein conformational characteristics related to thermostability
    • Querol, E., Perez-Pons, J.A.& Mozo-Villarias, A. Analysis of protein conformational characteristics related to thermostability. Protein Erg. 9, 265-271 (1996).
    • (1996) Protein Erg. , vol.9 , pp. 265-271
    • Querol, E.1    Perez-Pons, J.A.2    Mozo-Villarias, A.3
  • 28
    • 0031580199 scopus 로고    scopus 로고
    • Protein thermal stability, hydrogen bonds, and ion pairs
    • Vogt, G., Woell, S.& Argos, P. Protein thermal stability, hydrogen bonds, and ion pairs. J. Mol. Biol. 269, 631-643 (1997).
    • (1997) J. Mol. Biol. , vol.269 , pp. 631-643
    • Vogt, G.1    Woell, S.2    Argos, P.3
  • 29
    • 0031059866 scopus 로고    scopus 로고
    • Proceeding of X-ray diffraction data collected in oscillation mode
    • Otwinowski, Z.& Minor, W. Proceeding of X-ray diffraction data collected in oscillation mode. Methods Enzymol. 276.307-326 (1997).
    • (1997) Methods Enzymol. , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 30
    • 0028103275 scopus 로고
    • CCP4 suite: Programs for protein crystallography
    • Collaborative Computational Project Number 4. CCP4 suite: programs for protein crystallography. Acta Crystallogr. D 50, 760-763 (1994).
    • (1994) Acta Crystallogr. D , vol.50 , pp. 760-763
  • 31
    • 33847566866 scopus 로고
    • O version 5.9 Uppsala University, Uppsala, Sweden
    • Jones, T.A. & Kjeldgaard, M. O version 5.9 (Uppsala University, Uppsala, Sweden; 1993).
    • (1993)
    • Jones, T.A.1    Kjeldgaard, M.2
  • 33
    • 0028437737 scopus 로고
    • & Smit, E.L Simple and rapid determination of phytase activity
    • Engelen, A.J., van der Heeft, F.C., Randsdorp, P.M. & Smit, E.L Simple and rapid determination of phytase activity. J.AOAC Int. 77, 760-764 (1994).
    • (1994) J.AOAC Int. , vol.77 , pp. 760-764
    • Engelen, A.J.1    Van Der Heeft, F.C.2    Randsdorp, P.M.3
  • 34
    • 0030729838 scopus 로고    scopus 로고
    • An extensively modified version of MolScript that includes greatly enhanced coloring capabilities
    • Esnouf, R.M. An extensively modified version of MolScript that includes greatly enhanced coloring capabilities. J. Mol. Graph. Model. 15,132-134 (1997).
    • (1997) J. Mol. Graph. Model. , vol.15 , pp. 132-134
    • Esnouf, R.M.1
  • 35
    • 0028057108 scopus 로고
    • Raster3D version 2.0 -a program for photorealistic molecular graphics
    • Merritt, E.A.& Murphy, M.E.P. Raster3D version 2.0 -a program for photorealistic molecular graphics. Acta Crystallogr. D 50,869-873 (1994).
    • (1994) Acta Crystallogr. D , vol.50 , pp. 869-873
    • Merritt, E.A.1    Murphy, M.E.P.2
  • 36
    • 0029016182 scopus 로고
    • Classical electrostatics in biology and chemistry
    • Honig, B.& Nicholls, A. Classical electrostatics in biology and chemistry. Science 268,1144-1149(1995).
    • (1995) Science , vol.268 , pp. 1144-1149
    • Honig, B.1    Nicholls, A.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.