Helical Shifts Generate Two Distinct Conformers in the Atomic Resolution Structure of the CheA Phosphotransferase Domain from Thermotoga maritima

This publication has 55 references indexed in Scilit:

• Coiled-coils: stability, specificity, and drug delivery potential
  Advanced Drug Delivery Reviews, 2002
• Crystal Structure of the CheA Histidine Phosphotransfer Domain that Mediates Response Regulator Phosphorylation in Bacterial Chemotaxis
  Published by Elsevier ,2001
• Four-helical-bundle structure of the cytoplasmic domain of a serine chemotaxis receptor
  Nature, 1999
• Structure of CheA, a Signal-Transducing Histidine Kinase
  Cell, 1999
• Phosphotransfer Site of the Chemotaxis-Specific Protein Kinase CheA as Revealed by NMR
  Biochemistry, 1997
• Controlling Topology and Native-like Behavior of de Novo-Designed Peptides: Design and Characterization of Antiparallel Four-Stranded Coiled Coils
  Biochemistry, 1996
• NMR studies of the phosphotransfer domain of the histidine kinase CheA from Escherichia coli: assignments, secondary structure, general fold, and backbone dynamics
  Biochemistry, 1995
• The four‐lielix bundle: what determines a fold?
  The FASEB Journal, 1995
• Subunit interactions provide a significant contribution to the stability of the dimeric four-.alpha.-helical-bundle protein ROP
  Biochemistry, 1993
• Three-Dimensional Structures of the Ligand-Binding Domain of the Bacterial Aspartate Receptor with and Without a Ligand
  Science, 1991