Structure of the Conserved HAMP Domain in an Intact, Membrane-Bound Chemoreceptor: A Disulfide Mapping Study
- 10 November 2007
- journal article
- Published by American Chemical Society (ACS) in Biochemistry
- Vol. 46 (48), 13684-13695
- https://doi.org/10.1021/bi701832b
Abstract
No abstract availableKeywords
This publication has 27 references indexed in Scilit:
- Bacterial chemoreceptors: high-performance signaling in networked arraysTrends in Biochemical Sciences, 2008
- Use of Site‐Directed Cysteine and Disulfide Chemistry to Probe Protein Structure and Dynamics: Applications to Soluble and Transmembrane Receptors of Bacterial ChemotaxisMethods in Enzymology, 2007
- Evolutionary genomics reveals conserved structural determinants of signaling and adaptation in microbial chemoreceptorsProceedings of the National Academy of Sciences of the United States of America, 2007
- The HAMP Domain Structure Implies Helix Rotation in Transmembrane SignalingCell, 2006
- CheA Kinase of Bacterial Chemotaxis: Chemical Mapping of Four Essential Docking SitesBiochemistry, 2006
- Adaptation Mechanism of the Aspartate Receptor: Electrostatics of the Adaptation Subdomain Play a Key Role in Modulating Kinase ActivityBiochemistry, 2005
- SOCKET: a program for identifying and analysing coiled-coil motifs within protein structuresJournal of Molecular Biology, 2001
- The cytoplasmic helical linker domain of receptor histidine kinase and methyl-accepting proteins is common to many prokaryotic signalling proteinsFEMS Microbiology Letters, 1999
- Thermal motions of surface α-helices in the d-galactose chemosensory receptor: Detection by disulfide trappingJournal of Molecular Biology, 1992
- Three-Dimensional Structures of the Ligand-Binding Domain of the Bacterial Aspartate Receptor with and Without a LigandScience, 1991