Hyper-thermostability of CutA1 protein, with a denaturation temperature of nearly 150 degrees C.


Abstract

We found that the CutA1 protein, from Pyrococcus horikoshii (PhCutA1), has an extremely high denaturation temperature (T(d)) of nearly 150 degrees C, which exceeds the highest record determined by DSC by about 30 degrees C. To elucidate the mechanism of the ultra-high stability of PhCutA1, we analyzed the crystal structures of CutA1 proteins from three different sources, P. horikoshii, Thermus thermophilus, and Escherichia coli, with different growth temperatures (98, 75, and 37 degrees C). This analysis revealed that the remarkably increased number of ion pairs in the monomeric structure contributes to the stabilization of the trimeric structure and plays an important role in enhancing the T(d), up to 150 degrees C, for PhCutA1. Study holds ProTherm entries: 22918, 22919, 22920 Extra Details: Protein stability; DSC; Hyperthermophile; Heat denaturation; Ion pairs; Protein structure

Submission Details

ID: ADVT6SF6

Submitter: Connie Wang

Submission Date: April 24, 2018, 8:54 p.m.

Version: 1

Publication Details
Tanaka T;Sawano M;Ogasahara K;Sakaguchi Y;Bagautdinov B;Katoh E;Kuroishi C;Shinkai A;Yokoyama S;Yutani K,FEBS Lett. (2006) Hyper-thermostability of CutA1 protein, with a denaturation temperature of nearly 150 degrees C. PMID:16831434
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
1NZA 2003-02-17T00:00:00+0000 1.7 Divalent cation tolerance protein (Cut A1) from thermus thermophilus HB8
1V6H 2003-11-29T00:00:00+0000 1.9 The Trimeric Structure Of Divalent Cation Tolerance Protein CutA1 From Thermus Thermophilus HB8
4ZK7 2015-04-30T00:00:00+0000 3.4 Crystal structure of rescued two-component self-assembling tetrahedral cage T33-31
1J2V 2003-01-11T00:00:00+0000 2.0 Crystal Structure of CutA1 from Pyrococcus Horikoshii
1UKU 2003-09-01T00:00:00+0000 1.45 Crystal Structure of Pyrococcus horikoshii CutA1 Complexed with Cu2+
1UMJ 2003-10-02T00:00:00+0000 1.6 Crystal structure of Pyrococcus horikoshii CutA in the presence of 3M guanidine hydrochloride
2E66 2006-12-25T00:00:00+0000 2.0 Crystal Structure Of CutA1 From Pyrococcus Horikoshii OT3, Mutation D60A
4NYO 2013-12-11T00:00:00+0000 1.8 The 1.8 Angstrom Crystal Structure of the Periplasmic Divalent Cation Tolerance Protein Cuta from Pyrococcus Horikoshii OT3
4NYP 2013-12-11T00:00:00+0000 2.0 The 2.0 Angstrom Crystal Structure of Pyrococcus Horikoshii Cuta1 Complexed With NA+

Relevant UniProtKB Entries

Percent Identity Matching Chains Protein Accession Entry Name
100.0 Divalent-cation tolerance protein CutA Q7SIA8 CUTA_THET8
100.0 Divalent-cation tolerance protein CutA O58720 CUTA_PYRHO