The Mechanisms of HAMP-Mediated Signaling in Transmembrane Receptors

被引：80

作者：

Ferris, Hedda U. ^{[1
]}

Dunin-Horkawicz, Stanislaw ^{[1
]}

Mondejar, Laura Garcia ^{[2
]}

Hulko, Michael ^{[1
]}

Hantke, Klaus ^{[2
]}

Martin, Joerg ^{[1
]}

Schultz, Joachim E. ^{[2
]}

Zeth, Kornelius ^{[1
]}

Lupas, Andrei N. ^{[1
]}

Coles, Murray ^{[1
]}

机构：

[1] Max Planck Inst Dev Biol, Dept Prot Evolut, D-72076 Tubingen, Germany

[2] Univ Tubingen, Sch Pharm, Dept Pharmaceut Biochem, D-72076 Tubingen, Germany

来源：

STRUCTURE | 2011年 / 19卷 / 03期

关键词：

ESCHERICHIA-COLI; DOMAIN; PROTEIN; CHEMORECEPTORS; TRANSDUCTION; ASPARTATE; PROGRAM; KINASE; LINKER; ENVZ;

D O I：

10.1016/j.str.2011.01.006

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

HAMP domains mediate signal transduction in over 7500 enzyme-coupled receptors represented in all kingdoms of life. The HAMP domain of the putative archaeal receptor Af1503 has a parallel, dimeric, four-helical coiled coil structure, but with unusual core packing, related to canonical packing by concerted axial rotation of the helices. This has led to the gearbox model for signal transduction, whereby the alternate packing modes correspond to signaling states. Here we present structures of a series of Af1503 HAMP variants. We show that substitution of a conserved small side chain within the domain core (A291) for larger residues induces a gradual transition in packing mode, involving both changes in helix rotation and bundle shape, which are most prominent at the C-terminal, output end of the domain. These are correlated with activity and ligand response in vitro and in vivo by incorporating Af1503 HAMP into mycobacterial adenylyl cyclase assay systems.

引用

页码：378 / 385

页数：8

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