Crystal structure of phytase from Aspergillus ficuum at 2.5 Å resolution

Phytase is a high molecular weight acid phosphatase. The structure has an alpha/beta-domain similar to that of rat acid phosphatase and an alpha-domain with a new fold.

[1]  J. Vincent,et al.  Hydrolysis of phosphate monoesters: a biological problem with multiple chemical solutions. , 1992, Trends in biochemical sciences.

[2]  H. Watson,et al.  Structure and activity of phosphoglycerate mutase. , 1981, Philosophical transactions of the Royal Society of London. Series B, Biological sciences.

[3]  Axel T. Brunger,et al.  X-PLOR Version 3.1: A System for X-ray Crystallography and NMR , 1992 .

[4]  Axel T. Brunger,et al.  Model bias in macromolecular crystal structures , 1992 .

[5]  E. Myers,et al.  Basic local alignment search tool. , 1990, Journal of molecular biology.

[6]  I. Rayment,et al.  Molecular structure of an apolipoprotein determined at 2.5-A resolution. , 1991, Biochemistry.

[7]  Paul R. Gerber,et al.  MAB, a generally applicable molecular force field for structure modelling in medicinal chemistry , 1995, J. Comput. Aided Mol. Des..

[8]  K. Diederichs Structural superposition of proteins with unknown alignment and detection of topological similarity using a six‐dimensional search algorithm , 1995, Proteins.

[9]  Wolfgang Kabsch,et al.  Evaluation of Single-Crystal X-ray Diffraction Data from a Position-Sensitive Detector , 1988 .

[10]  A. H. Ullah,et al.  Extracellular phytase (E.C. 3.1.3.8) from Aspergillus ficuum NRRL 3135: purification and characterization. , 1987, Preparative biochemistry.

[11]  R. V. Etten,et al.  HUMAN PROSTATIC ACID PHOSPHATASE: A HISTIDINE PHOSPHATASE * , 1982, Annals of the New York Academy of Sciences.

[12]  H. Macarthur,et al.  Covalent structure, disulfide bonding, and identification of reactive surface and active site residues of human prostatic acid phosphatase. , 1991, The Journal of biological chemistry.

[13]  A. H. Ullah,et al.  Substrate selectivity in Aspergillus ficuum phytase and acid phosphatases using myo-inositol phosphates , 1994 .

[14]  G. Barton,et al.  A structural analysis of phosphate and sulphate binding sites in proteins. Estimation of propensities for binding and conservation of phosphate binding sites. , 1994, Journal of molecular biology.

[15]  A. H. Ullah,et al.  Aspergillus ficuum phytase: partial primary structure, substrate selectivity, and kinetic characterization. , 1988, Preparative biochemistry.

[16]  P. Kraulis A program to produce both detailed and schematic plots of protein structures , 1991 .

[17]  R. Huber,et al.  Accurate Bond and Angle Parameters for X-ray Protein Structure Refinement , 1991 .

[18]  G J Williams,et al.  The Protein Data Bank: a computer-based archival file for macromolecular structures. , 1977, Journal of molecular biology.

[19]  B. Matthews Solvent content of protein crystals. , 1968, Journal of molecular biology.

[20]  T. A. Jones,et al.  Using known substructures in protein model building and crystallography. , 1986, The EMBO journal.

[21]  G. Schneider,et al.  Three‐dimensional structure of rat acid phosphatase. , 1993, The EMBO journal.

[22]  R. Read Improved Fourier Coefficients for Maps Using Phases from Partial Structures with Errors , 1986 .

[23]  A T Brünger,et al.  Protein hydration observed by X-ray diffraction. Solvation properties of penicillopepsin and neuraminidase crystal structures. , 1994, Journal of molecular biology.

[24]  A. H. Ullah,et al.  Identification of Residues Involved in Active‐Site Formation in Aspergillus ficuum Phytase , 1992, Annals of the New York Academy of Sciences.

[25]  M. Karplus,et al.  Crystallographic R Factor Refinement by Molecular Dynamics , 1987, Science.

[26]  A. Brunger Free R value: a novel statistical quantity for assessing the accuracy of crystal structures. , 1992 .

[27]  F. Winkler,et al.  Mg2+ binding to the active site of EcoRV endonuclease: a crystallographic study of complexes with substrate and product DNA at 2 A resolution. , 1995, Biochemistry.

[28]  J. Thornton,et al.  Stereochemical quality of protein structure coordinates , 1992, Proteins.

[29]  M. Zhou,et al.  Overexpression, site-directed mutagenesis, and mechanism of Escherichia coli acid phosphatase. , 1992, The Journal of biological chemistry.

[30]  Amos Bairoch,et al.  The PROSITE database, its status in 1995 , 1996, Nucleic Acids Res..

[31]  J. Zou,et al.  Improved methods for building protein models in electron density maps and the location of errors in these models. , 1991, Acta crystallographica. Section A, Foundations of crystallography.