Structural features and signalling mechanisms of transmembrane chemoreceptors identified utilizing Nanodiscs
Transmembrane chemoreceptors are central components in the sensory system that mediates bacterial chemotaxis. Like many transmembrane proteins, these receptors are fully active only if inserted in a lipid bilayer. This requirement presents a challenge for in vitro analysis by many biochemical and structural techniques. The challenge is met by Nanodiscs, soluble, nanoscale (~10 nm diameter) particles of lipid bilayer surrounded by an annulus of amphipathic protein into which transmembrane proteins can be incorporated. Using Nanodiscs, we documented that chemoreceptor dimers bend at a specific locus along their 300 Å long axis, discovered that conformational differences between chemoreceptor signalling states were differential propensities of receptor helices to become momentarily unstructured, and determined that chemoreceptor signalling complexes activate and control the chemotaxis histidine kinase by altering its catalytic rate constant.
Date:
6 May 2016, 11:00 (Friday, 2nd week, Trinity 2016)
Venue:
Dorothy Crowfoot Hodgkin Building, off South Parks Road OX1 3QU
Venue Details:
Main Seminar Room
Speaker:
Gerald Hazelbauer (University of Missouri)
Organising department:
Department of Biochemistry
Organisers:
Dr Elena Seraidake (University of Oxford),
Dr Phillip Stansfeld (University of Oxford)
Host:
Judy Armitage (Biochemistry)
Part of:
SBMB Seminar Series (pre Oct 2018)
Booking required?:
Not required
Audience:
Members of the University only
Editor:
Phillip Stansfeld
