Cold denaturation-induced conformational changes in phosphoglycerate kinase from yeast.


Abstract

The temperature-dependent conformational equilibrium of 3-phosphoglycerate kinase has been studied in the temperature range from 1 to 30 degrees C by means of dynamic light scattering, small-angle X-ray scattering, differential scanning calorimetry, circular dichroism spectroscopy, and fluorescence spectroscopy. At 28 degrees C and in the presence of 0.7 M guanidine hydrochloride (GuHCl), the radius of gyration (RG) and the Stokes radius (RS) are 2.44 and 3.09 nm, respectively. Decreasing the temperature effects unfolding of the molecule, a process that involves two stages. The two stages correspond to the successive unfolding of the N-terminal and C-terminal domains. The peak maxima of the excess heat capacity, determined from differential calorimetric scans, extrapolated to 0 scan rate, are positioned at 16.5 degrees C for the N-terminal domain and at 6.3 degrees C for the C-terminal domain. At 4.5 degrees C, the radius of gyration and the Stokes radius increase to 7.8 and 4.8 nm, respectively. The persistence length and the length of the statistical chain segment of the unfolded polypeptide chain are 1.74 and 3.48 nm, corresponding to five and ten amino acids, respectively. At 1 degrees C, the dimensions of the unfolded chain nearly agree with the predicted dimensions under theta conditions. Thus, the conformational changes upon cold denaturation can be described by a transition from a compactly folded molecule to a random coil. The conformation-dependent ratio rho = RGRS-1 increases from rho = 0.79 to rho = 1.63. The volume of the unfolded chain is 30 times larger than that of the folded chain in the native state.(ABSTRACT TRUNCATED AT 250 WORDS) Study holds ProTherm entries: 4560 Extra Details: additive : EDTA(10 mM), temperature-dependent; persistence length; slow kinetics;,conformational changes

Submission Details

ID: tfJvnz9S

Submitter: Connie Wang

Submission Date: April 24, 2018, 8:26 p.m.

Version: 1

Publication Details
Damaschun G;Damaschun H;Gast K;Misselwitz R;Müller JJ;Pfeil W;Zirwer D,Biochemistry (1993) Cold denaturation-induced conformational changes in phosphoglycerate kinase from yeast. PMID:8347582
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
1FW8 2001-03-22 2.3 CIRCULARLY PERMUTED PHOSPHOGLYCERATE KINASE FROM YEAST: PGK P72
1QPG 1996-06-10 2.4 3-PHOSPHOGLYCERATE KINASE, MUTATION R65Q
3PGK 1982-09-24 2.5 The structure of yeast phosphoglycerate kinase at 0.25 nm resolution

Relevant UniProtKB Entries

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