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          Document History for Document ID 305896

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Document Version Version Comment Date Status
305896.0 [No comment] 20.03.2013 11:45 Released

ID: 305896.0, MPI für Entwicklungsbiologie / Abteilung 1 - Protein Evolution (A. Lupas)
The HAMP domain structure implies helix rotation in transmembrane signaling.
Authors:Hulko, Michael; Berndt, F.; Gruber, Markus; Linder, J. U.; Truffault, Vincent; Schultz, A.; Martin, Joerg; Lupas, Andrei; Coles, Murray
Language:English
Date of Publication (YYYY-MM-DD):2006-09-08
Title of Journal:Cell
Volume:126
Issue / Number:(5)
Start Page:929
End Page:940
Sequence Number of Article:16959572
Review Status:not specified
Audience:Not Specified
Abstract / Description:HAMP domains connect extracellular sensory with intracellular signaling domains in over 7500 proteins, including histidine kinases, adenylyl cyclases, chemotaxis receptors, and phosphatases. The solution structure of an archaeal HAMP domain shows a homodimeric, four-helical, parallel coiled coil with unusual interhelical packing, related to the canonical packing by rotation of the helices. This suggests a model for the mechanism of signal transduction, in which HAMP alternates between the observed conformation and a canonical coiled coil. We explored this mechanism in vitro and in vivo using HAMP domain fusions with a mycobacterial adenylyl cyclase and an E. coli chemotaxis receptor. Structural and functional studies show that the equilibrium between the two forms is dependent on the side-chain size of residue 291, which is alanine in the wild-type protein.
External Publication Status:published
Document Type:Article
Affiliations:MPI für Entwicklungsbiologie/Abteilung 1 - Proteinevolution (Andrei Lupas)