Crystal structure of a phosphatase-resistant mutant of sporulation response regulator Spo0F from Bacillus subtilis.

[1]  K. Varughese,et al.  Calcium binding cyclic hexapeptide. Crystal structure of cyclo-(L-prolyl-glycyl)3 calcium complex. , 2009, International journal of peptide and protein research.

[2]  N. Xuong,et al.  Crystallization and preliminary X-ray analysis of a Y13S mutant of Spo0F from Bacillus subtilis. , 1996, Acta crystallographica. Section D, Biological crystallography.

[3]  J. Hoch,et al.  A phosphotransferase activity of the Bacillus subtilis sporulation protein Spo0F that employs phosphoramidate substrates. , 1996, Biochemistry.

[4]  J. Hoch,et al.  Cell-cell communication regulates the effects of protein aspartate phosphatases on the phosphorelay controlling development in Bacillus subtilis. , 1996, Proceedings of the National Academy of Sciences of the United States of America.

[5]  L. Kay,et al.  Nuclear magnetic resonance assignments and global fold of a CheY-binding domain in CheA, the chemotaxis-specific kinase of Escherichia coli. , 1995, Biochemistry.

[6]  P. Matsumura,et al.  Mutations Leading to Altered CheA Binding Cluster on a Face of CheY (*) , 1995, The Journal of Biological Chemistry.

[7]  Frederick W. Dahlquist,et al.  Localized perturbations in CheY structure monitored by NMR identify a CheA binding interface , 1995, Nature Structural Biology.

[8]  L. Amzel,et al.  The three-dimensional structure of NAD(P)H:quinone reductase, a flavoprotein involved in cancer chemoprotection and chemotherapy: mechanism of the two-electron reduction. , 1995, Proceedings of the National Academy of Sciences of the United States of America.

[9]  J. Hoch,et al.  1H, 15N, and 13C backbone chemical shift assignments, secondary structure, and magnesium‐binding characteristics of the bacillus subtilis response regulator, SpoOF, determined by heteronuclear high‐resolution NMR , 1995, Protein science : a publication of the Protein Society.

[10]  P. Matsumura,et al.  Uncoupled Phosphorylation and Activation in Bacterial Chemotaxis , 1995, The Journal of Biological Chemistry.

[11]  P. Alzari,et al.  Structural and Functional Analysis of the Metal-binding Sites of Clostridium thermocellum Endoglucanase CelD (*) , 1995, The Journal of Biological Chemistry.

[12]  M. Simon,et al.  Mutations in the chemotactic response regulator, CheY, that confer resistance to the phosphatase activity of CheZ , 1995, Molecular microbiology.

[13]  R. Liddington,et al.  Crystal structure of the A domain from the a subunit of integrin CR3 (CD11 b/CD18) , 1995, Cell.

[14]  Philippe Glaser,et al.  Multiple protein-aspartate phosphatases provide a mechanism for the integration of diverse signals in the control of development in B. subtilis , 1994, Cell.

[15]  F. Dahlquist,et al.  Assignments, secondary structure, global fold, and dynamics of chemotaxis Y protein using three- and four-dimensional heteronuclear (13C,15N) NMR spectroscopy. , 1994, Biochemistry.

[16]  P. Nordlund,et al.  The crystal structure of a low-molecular-weight phosphotyrosine protein phosphatase , 1994, Nature.

[17]  J. Hoch,et al.  Subunit composition and domain structure of the Spo0A sporulation transcription factor of Bacillus subtilis. , 1994, The Journal of biological chemistry.

[18]  P. Chakrabarti.  Conformational analysis of carboxylate and carboxamide side-chains bound to cations. , 1994, Journal of Molecular Biology.

[19]  J. Thornton,et al.  Satisfying hydrogen bonding potential in proteins. , 1994, Journal of molecular biology.

[20]  L. Serrano,et al.  Magnesium binding to the bacterial chemotaxis protein CheY results in large conformational changes involving its functional surface. , 1994, Journal of Molecular Biology.

[21]  G. Petsko,et al.  Structure of the Mg(2+)-bound form of CheY and mechanism of phosphoryl transfer in bacterial chemotaxis. , 1994, Biochemistry.

[22]  K. Volz,et al.  Structural conservation in the CheY superfamily. , 1993, Biochemistry.

[23]  M Welch,et al.  Phosphorylation-dependent binding of a signal molecule to the flagellar switch of bacteria. , 1993, Proceedings of the National Academy of Sciences of the United States of America.

[24]  M. Simon,et al.  Activation of the phosphosignaling protein CheY. II. Analysis of activated mutants by 19F NMR and protein engineering. , 1993, The Journal of biological chemistry.

[25]  S V Evans,et al.  SETOR: hardware-lighted three-dimensional solid model representations of macromolecules. , 1993, Journal of molecular graphics.

[26]  J. Thornton,et al.  PROCHECK: a program to check the stereochemical quality of protein structures , 1993 .

[27]  P. Matsumura,et al.  Crystal structure of Escherichia coli CheY refined at 1.7-A resolution. , 1993, The Journal of biological chemistry.

[28]  D. Koshland,et al.  Phosphorylation site of NtrC, a protein phosphatase whose covalent intermediate activates transcription , 1992, Journal of bacteriology.

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

[30]  J. Stock,et al.  Roles of the highly conserved aspartate and lysine residues in the response regulator of bacterial chemotaxis. , 1991, The Journal of biological chemistry.

[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.

[32]  J. Hoch,et al.  Initiation of sporulation in B. subtilis is controlled by a multicomponent phosphorelay , 1991, Cell.

[33]  J. Stock,et al.  Signal transduction in bacteria , 1990, Nature.

[34]  D E Koshland,et al.  Identification of the site of phosphorylation of the chemotaxis response regulator protein, CheY. , 1989, The Journal of biological chemistry.

[35]  A. Ninfa,et al.  Protein phosphorylation and regulation of adaptive responses in bacteria. , 1989, Microbiological reviews.

[36]  C. Schutt,et al.  Three-dimensional structure of CheY, the response regulator of bacterial chemotaxis , 1989, Nature.

[37]  C. Cambillau,et al.  TOM: a FRODO subpackage for protein-ligand fitting with interactive energy minimization , 1988 .

[38]  Robert B. Bourret,et al.  Histidine phosphorylation and phosphoryl group transfer in bacterial chemotaxis , 1988, Nature.

[39]  Brian W. Matthews,et al.  An efficient general-purpose least-squares refinement program for macromolecular structures , 1987 .

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

[41]  J. Stock,et al.  Multiple forms of the CheB methylesterase in bacterial chemosensing. , 1985, The Journal of biological chemistry.

[42]  D I Stuart,et al.  Crystal structure of cat muscle pyruvate kinase at a resolution of 2.6 A. , 1979, Journal of molecular biology.

[43]  R. M. Burnett,et al.  The structure of the oxidized form of clostridial flavodoxin at 1.9-A resolution. , 1974, The Journal of biological chemistry.

[44]  B. Lee,et al.  The interpretation of protein structures: estimation of static accessibility. , 1971, Journal of molecular biology.

[45]  V. Luzzati,et al.  Traitement statistique des erreurs dans la determination des structures cristallines , 1952 .

[46]  W Furey,et al.  PHASES-95: a program package for processing and analyzing diffraction data from macromolecules. , 1997, Methods in enzymology.

[47]  M. Surette,et al.  Two-component signal transduction systems : structure-function relationships and mechanisms of catalysis , 1995 .

[48]  K. Volz.  Structural and Functional Conservation in Response Regulators , 1995 .

[49]  J. Hoch.  Regulation of the phosphorelay and the initiation of sporulation in Bacillus subtilis. , 1993, Annual review of microbiology.

[50]  J. S. Parkinson,et al.  Communication modules in bacterial signaling proteins. , 1992, Annual review of genetics.

[51]  B. C. Wang.  Resolution of phase ambiguity in macromolecular crystallography. , 1985, Methods in enzymology.

[52]  R. Hamlin,et al.  [27] Multiwire area X-ray diffractometers , 1985 .

[53]  N. Xuong,et al.  Software for a diffractometer with multiwire area detector. , 1985, Methods in enzymology.

[54]  J. Richardson,et al.  The anatomy and taxonomy of protein structure. , 1981, Advances in protein chemistry.

[55]  J. Knowles.  Enzyme-catalyzed phosphoryl transfer reactions. , 1980, Annual review of biochemistry.

[56]  G. N. Ramachandran,et al.  Conformation of polypeptides and proteins. , 1968, Advances in protein chemistry.