CaltechAUTHORS
  A Caltech Library Service

Electrostatics Facilitates the Trimer-of-Dimers Formation of the Chemoreceptor Signaling Domain

Petukh, Marharyta and Ortega, Davi and Zhulin, Igor B. (2017) Electrostatics Facilitates the Trimer-of-Dimers Formation of the Chemoreceptor Signaling Domain. Biophysical Journal, 112 (3, Supp. 1). 89a. ISSN 0006-3495. https://resolver.caltech.edu/CaltechAUTHORS:20170623-102827178

Full text is not posted in this repository. Consult Related URLs below.

Use this Persistent URL to link to this item: https://resolver.caltech.edu/CaltechAUTHORS:20170623-102827178

Abstract

Chemoreceptors are crucial components of the bacterial sensory system that modulates cellular motility. They detect changes in the environment and transmit information to CheA histidine kinase, which ultimately controls cellular flagellar motors. The prototypical Tsr chemoreceptor in E. coli is a homodimer containing two principle functional modules: (i) a periplasmic ligand-binding domain and (ii) a cytoplasmic signaling domain comprising an antiparallel, four-helix coiled-coil bundle. Receptor dimers are arranged into a trimer-of-dimers, which is a minimal physical unit essential for enhancing the CheA activity several hundredfold. Recent advances in cryo-electron tomography showed that trimers-of-dimers are arranged into highly ordered hexagon arrays at the cell pole; however, the mechanism underlying the trimer-of-dimer and higher order array formation remains unknown. Current evidence from structural and biochemical studies suggest that trimers-of-dimers are maintained exclusively by contacts at the chemoreceptor cytoplasmic tip. Here, using all-atom, microsecond-range MD simulation of the Tsr trimer-of-dimers crystal structure, we show that dimers within the trimer may interact throughout the entire length of the signaling domain. While inter-dimer contacts at the chemoreceptor tip occur via hydrophobic interactions, complete dimer “zipping” is facilitated by electrostatics, especially by the polar solvation component. We also show that many of the residues involved in establishing hydrogen bonds and salt bridges between dimers are evolutionary conserved.


Item Type:Article
Related URLs:
URLURL TypeDescription
https://doi.org/10.1016/j.bpj.2016.11.523DOIArticle
http://www.sciencedirect.com/science/article/pii/S0006349516315533PublisherArticle
ORCID:
AuthorORCID
Ortega, Davi0000-0002-8344-2335
Additional Information:© 2017 Elsevier B.V. Available online 3 February 2017. Meeting Abstract: 454-Pos.
Issue or Number:3, Supp. 1
Record Number:CaltechAUTHORS:20170623-102827178
Persistent URL:https://resolver.caltech.edu/CaltechAUTHORS:20170623-102827178
Official Citation:Marharyta Petukh, Davi Ortega, Igor B. Zhulin, Electrostatics Facilitates the Trimer-of-Dimers Formation of the Chemoreceptor Signaling Domain, Biophysical Journal, Volume 112, Issue 3, Supplement 1, 3 February 2017, Page 89a, ISSN 0006-3495, https://doi.org/10.1016/j.bpj.2016.11.523. (http://www.sciencedirect.com/science/article/pii/S0006349516315533)
Usage Policy:No commercial reproduction, distribution, display or performance rights in this work are provided.
ID Code:78512
Collection:CaltechAUTHORS
Deposited By: Tony Diaz
Deposited On:24 Jun 2017 03:05
Last Modified:03 Oct 2019 18:09

Repository Staff Only: item control page