The structure of a soluble chemoreceptor suggests a mechanism for propagating conformational signals.

Abstract:

:Transmembrane chemoreceptors, also known as methyl-accepting chemotaxis proteins (MCPs), translate extracellular signals into intracellular responses in the bacterial chemotaxis system. MCP ligand binding domains control the activity of the CheA kinase, situated approximately 200 A away, across the cytoplasmic membrane. The 2.17 A resolution crystal structure of a Thermotoga maritima soluble receptor (Tm14) reveals distortions in its dimeric four-helix bundle that provide insight into the conformational states available to MCPs for propagating signals. A bulge in one helix generates asymmetry between subunits that displaces the kinase-interacting tip, which resides more than 100 A away. The maximum bundle distortion maps to the adaptation region of transmembrane MCPs where reversible methylation of acidic residues tunes receptor activity. Minor alterations in coiled-coil packing geometry translate the bulge distortion to a >25 A movement of the tip relative to the bundle stalks. The Tm14 structure discloses how alterations in local helical structure, which could be induced by changes in methylation state and/or by conformational signals from membrane proximal regions, can reposition a remote domain that interacts with the CheA kinase.

journal_name

Biochemistry

journal_title

Biochemistry

authors

Pollard AM,Bilwes AM,Crane BR

doi

10.1021/bi801727m

subject

Has Abstract

pub_date

2009-03-10 00:00:00

pages

1936-44

issue

9

eissn

0006-2960

issn

1520-4995

pii

10.1021/bi801727m

journal_volume

48

pub_type

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