Towards understanding a molecular switch mechanism: Thermodynamic and crystallographic studies of the signal transduction protein CheY

Journal of Molecular Biology

Volumn 303, Issue 2, 2000, Pages 213-225

  Solà, Maria ^a   López Hernández, Eva ^b   Cronet, Philippe ^b   Lacroix, Emmanuel ^b   Serrano, Luis ^b   Coll, Miquel ^a   Párraga, Antonio ^a  

^a INSTITUT DE BIOLOGIA MOLECULAR DE BARCELONA   (Spain)

^b EUROPEAN MOLECULAR BIOLOGY LABORATORY   (Germany)

Author keywords

Chemotaxis; CheY; Crystal structure; Signal transduction; Stability

Indexed keywords

ALPHA HELIX; ANIMAL CELL; ARTICLE; CHEMOTAXIS; CRYSTAL STRUCTURE; ENZYME ACTIVE SITE; GENE SWITCHING; MEMBRANE BINDING; NONHUMAN; PRIORITY JOURNAL; PROTEIN PROTEIN INTERACTION; PROTEIN STABILITY; SIGNAL TRANSDUCTION; THERMODYNAMICS; X RAY CRYSTALLOGRAPHY;

ANIMALIA;

EID: 0034692882     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.2000.4507     Document Type: Article

References (56)

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3. Magnesium binding to the bacterial chemotaxis protein CheY results in large conformational changes involving its functional surface
4. The three-dimensional structure of two mutants of the signal transduction protein CheY suggest its molecular activation mechanism
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12. Histidine phosphorylation and phosphoryl group transfer in bacterial chemotaxis
13. Evaluation of single crystal X-ray diffraction from a position-sensitive detector
14. Bivalent-metal binding to CheY protein. Effect on protein conformation
15. Structure of a transiently phosphorylated switch in bacterial signal transduction
16. MOLMOL: A program for display and analysis of macromolecular structures
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19. Structure of the transition state for folding of the 129 aa protein CheY resembles that of a smaller protein, CI-2
20. Folding kinetics of CheY mutants with enhanced native alpha-helix propensities
21. Divalent metal ion binding to the CheY protein and its significance to phosphotransfer in bacterial chemotaxis
22. Roles of the highly conserved aspartate and lysine residues in the response regulator of bacterial chemotaxis
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24. Solvent content of protein crystals
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27. Effect of active site residues in barnase on activity and stability
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30. Structural analysis of peptides encompassing all alpha-helices of three alpha/beta parallel proteins: Che-Y, flavodoxin and P21-ras: Implications for alpha,helix stability and the folding of alpha/ beta parallel proteins
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32. AMoRe: An automated package for molecular replacement
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35. Amino acid preferences for specific locations at the ends of alpha helices
36. A chemotactic signaling surface on CheY defined by suppressors of flagellar switch mutations
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39. Three-dimensional structure of chemotactic CheY protein in aqueous solution by nuclear magnetic resonance methods
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45. PROTEIN
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48. Stabilization of proteins by rational design of alpha-helix stability using helix/coil transition theory
49. Structural conservation in the CheY superfamily
50. Crystal structure of Escherichia coli CheY refined at 1.7-resolution
51. Structure of the CheY-binding domain of histidine kinase CheA in complex with CheY
52. Structure analysis of two CheY mutants: Importance of the hydrogen-bond contribution to protein stability
53. Tyrosine 106 of CheY plays an important role in chemotaxis signal transduction in Escherichia coll
54. Crystal structures of CheY mutants Y106W and T87I/Y106W
55. The Chez-binding surface of CheY overlaps the CheA- and FliM-binding surfaces