Cold denaturation of yeast phosphoglycerate kinase: which domain is more stable?


Under destabilising conditions both heat and cold denaturation of yeast phosphoglycerate kinase (PGK) can be observed. According to previous interpretation of experimental data and theoretical calculations, the C-terminal domain should be more stable than the N-terminal domain at all temperatures. We report on thermal unfolding experiments with PGK and its isolated domains, which give rise to a revision of this view. While the C-terminal domain is indeed the more stable one on heating, it reveals lower stability in the cold. These findings are of importance, because PGK has been frequently used as a model for protein folding and mutual domain interactions. Study holds ProTherm entries: 9841 Extra Details: additive : DTT(1 mM), protein folding; cold denaturation; domain interaction;,circular dichroism; differential scanning; calorimetry

Submission Details

ID: CCAioopK3

Submitter: Connie Wang

Submission Date: April 24, 2018, 8:38 p.m.

Version: 1

Publication Details
Gast K;Damaschun G;Desmadril M;Minard P;Müller-Frohne M;Pfeil W;Zirwer D,FEBS Lett. (1995) Cold denaturation of yeast phosphoglycerate kinase: which domain is more stable? PMID:7843410
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
1QPG 1996-01-04T00:00:00+0000 2.4 3-PHOSPHOGLYCERATE KINASE, MUTATION R65Q
3PGK 1982-07-15T00:00:00+0000 2.5 The structure of yeast phosphoglycerate kinase at 0.25 nm resolution

Relevant UniProtKB Entries

Percent Identity Matching Chains Protein Accession Entry Name
100.0 Phosphoglycerate kinase P00560 PGK_YEAST
94.5 Phosphoglycerate kinase Q6FKY1 PGK_CANGA