CaltechAUTHORS
  A Caltech Library Service

Crystal structures of CheY from Thermotoga maritima do not support conventional explanations for the structural basis of enhanced thermostability

Usher, Ken C. and de la Cruz, A. F. and Dahlquist, Frederick W. and Swanson, Ronald V. and Simon, Melvin I. and Remington, S. James (1998) Crystal structures of CheY from Thermotoga maritima do not support conventional explanations for the structural basis of enhanced thermostability. Protein Science, 7 (2). pp. 403-412. ISSN 0961-8368. PMCID PMC2143910. http://resolver.caltech.edu/CaltechAUTHORS:20170409-082224546

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

Use this Persistent URL to link to this item: http://resolver.caltech.edu/CaltechAUTHORS:20170409-082224546

Abstract

The crystal structure of CheY protein from Thermotoga maritima has been determined in four crystal forms with and without Mg++ bound, at up to 1.9 A resolution. Structural comparisons with CheY from Escherichia coli shows substantial similarity in their folds, with some concerted changes propagating away from the active site that suggest how phosphorylated CheY, a signal transduction protein in bacterial chemotaxis, is recognized by its targets. A highly conserved segment of the protein (the "y-turn loop," residues 55-61), previously suggested to be a rigid recognition determinant, is for the first time seen in two alternative conformations in the different crystal structures. Although CheY from Thermotoga has much higher thermal stability than its mesophilic counterparts, comparison of structural features previously proposed to enhance thermostability such as hydrogen bonds, ion pairs, compactness, and hydrophobic surface burial would not suggest it to be so.


Item Type:Article
Related URLs:
URLURL TypeDescription
http://dx.doi.org/10.1002/pro.5560070221DOIArticle
https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2143910/PubMed CentralArticle
Additional Information:© 1998 The Protein Society. (RECEIVED July 23, 1997; ACCEPTED October 30, 1997) This work was supported by National Science Foundation Grants MCB9418479 (S.J.R.), and MCB9604213 (F.W.D.).
Funders:
Funding AgencyGrant Number
NSFMCB-9418479
NSFMCB-9604213
Subject Keywords:chemotaxis, protein crystallography, signal transduction, thermostability
PubMed Central ID:PMC2143910
Record Number:CaltechAUTHORS:20170409-082224546
Persistent URL:http://resolver.caltech.edu/CaltechAUTHORS:20170409-082224546
Official Citation:Usher, K. C., De La Cruz, A. F., Dahlquist, F. W., James Remington, S. , Swanson, R. V. and Simon, M. I. (1998), Crystal structures of CheY from Thermotoga maritima do not support conventional explanations for the structural basis of enhanced thermostability. Protein Science, 7: 403-412. doi:10.1002/pro.5560070221
Usage Policy:No commercial reproduction, distribution, display or performance rights in this work are provided.
ID Code:76453
Collection:CaltechAUTHORS
Deposited By: 1Science Import
Deposited On:03 Apr 2018 22:25
Last Modified:03 Apr 2018 22:25

Repository Staff Only: item control page