Two crystal structures of pectin lyase A from Aspergillus reveal a pH driven conformational change and striking divergence in the substrate-binding clefts of pectin and pectate lyases.

[1]  R. Read.  Structure-factor probabilities for related structures , 1990 .

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

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

[4]  L. Lally.  The CCP 4 Suite — Computer programs for protein crystallography , 1998 .

[5]  J. Whitaker.  New and future uses of enzymes in food processing , 1990 .

[6]  Sung-Hou Kim,et al.  Sparse matrix sampling: a screening method for crystallization of proteins , 1991 .

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

[8]  N. Keen,et al.  The Role of Pectic Enzymes in Plant Pathogenesis , 1986 .

[9]  P. Kolattukudy,et al.  Pectate lyase from Fusarium solani f. sp. pisi: purification, characterization, in vitro translation of the mRNA, and involvement in pathogenicity. , 1987, Archives of biochemistry and biophysics.

[10]  M. Yoder,et al.  New domain motif: the structure of pectate lyase C, a secreted plant virulence factor. , 1993, Science.

[11]  V S Lamzin,et al.  Automated refinement of protein models. , 1993, Acta crystallographica. Section D, Biological crystallography.

[12]  B Henrissat,et al.  Functional Implications of Structure-Based Sequence Alignment of Proteins in the Extracellular Pectate Lyase Superfamily , 1995, Plant physiology.

[13]  M. Yoder,et al.  The Three-Dimensional Structure of Pectate Lyase E, a Plant Virulence Factor from Erwinia chrysanthemi , 1994, Plant physiology.

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

[15]  G. Birch,et al.  Enzymes and Food Processing , 1980 .

[16]  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.

[17]  F. V. Houdenhoven.  Studies on pectin lyase , 1975 .

[18]  F. Jurnak,et al.  Differential Effect of Site-directed Mutations in pelC on Pectate Lyase Activity, Plant Tissue Maceration, and Elicitor Activity* , 1996, The Journal of Biological Chemistry.

[19]  Functional and structural role of a tryptophan generally observed in protein-carbohydrate interaction. TRP-62 of hen egg white lysozyme. , 1994, The Journal of biological chemistry.

[20]  Howard J. Allen,et al.  Glycoconjugates : composition, structure, and function , 1992 .

[21]  J. Navaza,et al.  AMoRe: an automated package for molecular replacement , 1994 .

[22]  Crystallization and preliminary X-ray analysis of pectin lyase A from Aspergillus niger. , 1996, Acta crystallographica. Section D, Biological crystallography.

[23]  R. Pickersgill,et al.  The structure of Bacillus subtilis pectate lyase in complex with calcium , 1994, Nature Structural Biology.

[24]  F. Barras,et al.  EXTRACELLULAR ENZYMES AND PATHOGENESIS OF SOFT-ROT ERWINIA , 1994 .

[25]  Parallel beta-domains: a new fold in protein structures. , 1994, Current opinion in structural biology.

[26]  W. Pilnik,et al.  7 – PECTIC ENZYMES , 1979 .

[27]  T. Rafnar,et al.  Cloning of Amb a I (antigen E), the major allergen family of short ragweed pollen. , 1991, The Journal of biological chemistry.

[28]  M. Cygler,et al.  Recognition of a cell-surface oligosaccharide of pathogenic Salmonella by an antibody Fab fragment. , 1991, Science.

[29]  G. Kleywegt,et al.  Halloween ... Masks and Bones , 1994 .

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

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