Thermodynamic basis for the increased thermostability of CheY from the hyperthermophile Thermotoga maritima.


The CheY protein isolated from the hyperthermophile Thermotoga maritima is much more resistant to thermally induced unfolding than is its counterpart from the mesophile Bacillus subtilis. To determine the basis of this increased thermostability, the temperature dependence of the free energy of unfolding was determined for these CheY homologues using denaturant-induced unfolding experiments. This allowed comparison of T. maritima CheY with B. subtilis CheY and determination of the thermodynamic qualities responsible for the enhanced thermostability of T. maritima CheY. The stability of the thermophilic CheY protein is a direct result of the increased enthalpy contribution at the temperature of zero entropy, T(s), and the decreased heat capacity change upon unfolding, resulting in a decreased dependence of the free energy of unfolding on temperature. It was found that neither purely entropic nor purely enthalpic contributions alone (as reflected by T(s)) were sufficient to account for the increase in stability. Study holds ProTherm entries: 12272, 12273, 12274, 12275, 12276, 12277 Extra Details: hyperthermophile; free energy of unfolding; enthalpy

Submission Details

ID: jRMmcAL9

Submitter: Connie Wang

Submission Date: April 24, 2018, 8:43 p.m.

Version: 1

Publication Details
Deutschman WA;Dahlquist FW,Biochemistry (2001) Thermodynamic basis for the increased thermostability of CheY from the hyperthermophile Thermotoga maritima. PMID:11669649
Additional Information

Structure view and single mutant data analysis

Study data

No weblogo for data of varying length.
Colors: D E R H K S T N Q A V I L M F Y W C G P

Data Distribution

Studies with similar sequences (approximate matches)

Correlation with other assays (exact sequence matches)

Relevant PDB Entries

Structure ID Release Date Resolution Structure Title
1TMY 1997-05-16T00:00:00+0000 1.9 CHEY FROM THERMOTOGA MARITIMA (APO-I)
1U0S 2004-07-14T00:00:00+0000 1.9 Chemotaxis kinase CheA P2 domain in complex with response regulator CheY from the thermophile thermotoga maritima
2LLE 2011-11-07T00:00:00+0000 0 Computational design of an eight-stranded (beta/alpha)-barrel from fragments of different folds
2TMY 1997-05-19T00:00:00+0000 2.3 CHEY FROM THERMOTOGA MARITIMA (APO-II)
3TMY 1997-06-04T00:00:00+0000 2.2 CHEY FROM THERMOTOGA MARITIMA (MN-III)
4IGA 2012-12-17T00:00:00+0000 1.73 The crystal structure of an activated Thermotoga maritima CheY with N-terminal region of FliM
4QWV 2014-07-17T00:00:00+0000 2.45 A PBP-like protein built from fragments of different folds
4QYW 2014-07-25T00:00:00+0000 1.6 Structure of phosphono-CheY from T.maritima
4TMY 1997-06-06T00:00:00+0000 2.8 CHEY FROM THERMOTOGA MARITIMA (MG-IV)
6C40 2018-01-11T00:00:00+0000 2.7 CheY41PyTyrD54K from Thermotoga maritima

Relevant UniProtKB Entries

Percent Identity Matching Chains Protein Accession Entry Name
100.0 Chemotaxis protein CheY Q56312 CHEY_THEMA
100.0 Chemotaxis protein CheY P24072 CHEY_BACSU
100.0 Endolysin P00720 ENLYS_BPT4