2LFS

Solution structure of the chimeric Af1503 HAMP- EnvZ DHp homodimer; A219F variant

Summary for 2LFS

• Entry DOI: 10.2210/pdb2lfs/pdb
• Related: 2LFR 3ZRV 3ZRW 3ZRX
• NMR Information: BMRB: 17776
• Descriptor: HAMP domain-containing protein, Osmolarity sensor protein EnzV chimera (1 entity in total)
• Functional Keywords: transmembrane signaling, hamp domain, histidine kinase, gearbox model, transferase
• Biological source: Archaeoglobus fulgidus (strain ATCC 49558 / VC-16 / DSM 4304 / JCM 9628 / NBRC 100126); More
• Cellular location: Cell inner membrane; Multi-pass membrane protein (By similarity): P0AEJ5
• Total number of polymer chains: 2
• Total formula weight: 26007.55

Authors

Coles, M.,Ferris, H.U.,Hulko, M.,Martin, J.,Lupas, A.N. (deposition date: 2011-07-10, release date: 2011-08-24, Last modification date: 2024-05-15)

Primary citation

Ferris, H.U.,Dunin-Horkawicz, S.,Hornig, N.,Hulko, M.,Martin, J.,Schultz, J.E.,Zeth, K.,Lupas, A.N.,Coles, M.
Mechanism of regulation of receptor histidine kinases.
Structure, 20:56-66, 2012

PubMed Abstract: Bacterial transmembrane receptors regulate an intracellular catalytic output in response to extracellular sensory input. To investigate the conformational changes that relay the regulatory signal, we have studied the HAMP domain, a ubiquitous intracellular module connecting input to output domains. HAMP forms a parallel, dimeric, four-helical coiled coil, and rational substitutions in our model domain (Af1503 HAMP) induce a transition in its interhelical packing, characterized by axial rotation of all four helices (the gearbox signaling model). We now illustrate how these conformational changes are propagated to a downstream domain by fusing Af1503 HAMP variants to the DHp domain of EnvZ, a bacterial histidine kinase. Structures of wild-type and mutant constructs are correlated with ligand response in vivo, clearly associating them with distinct signaling states. We propose that altered recognition of the catalytic domain by DHp, rather than a shift in position of the phospho-accepting histidine, forms the basis for regulation of kinase activity.

PubMed: 22244755
DOI: 10.1016/j.str.2011.11.014

Experimental method

SOLUTION NMR