Glucose-induced thermal stabilization of the native conformation of GLUT 1.


Abstract

The glucose transporter, GLUT 1, was purified from erythrocyte membranes and incorporated into vesicles of erythrocyte lipids. These protein-containing vesicles were studied with differential scanning calorimetry. It was found that the protein underwent an irreversible denaturation at 68.5 +/- 0.2 degreesC (at a scan rate of 0.25 degreesC/min) which was shifted to 72.6 +/- 0.2 degreesC in the presence of 500 mM D-glucose, while 500 mM L-glucose or 10 microM cytochalasin B did not produce a significant shift. The calorimetric enthalpy was found to be 150 kcal/mol, independent of the presence of D-glucose. On a weight basis this value is lower than that for soluble proteins, but it is comparable to values obtained with other integral membrane proteins. The van't Hoff enthalpy is similar to the calorimetric enthalpy, within the experimental error, indicating that the transition is not likely to be cooperative. The activation energy is estimated from both the scan rate dependence of the transition temperature and from the shape of the DSC curve. The presence of 500 mM D-glucose slightly decreases the activation energy. It is concluded that the shift to a higher denaturation transition temperature in the presence of D-glucose is not a result of increased kinetic stability of GLUT 1. Study holds ProTherm entries: 23801, 23802, 23803, 23804, 23805, 23806, 23807, 23808 Extra Details: additive:glucose(0 mM), scan rate:0.25 C/min glucose transporter-GLUT1, D-glucose, kinetic stability.

Submission Details

ID: 5Vyw6oCU4

Submitter: Connie Wang

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

Version: 1

Publication Details
Epand RF;Epand RM;Jung CY,Biochemistry (1999) Glucose-induced thermal stabilization of the native conformation of GLUT 1. PMID:9890928
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
5EQG 2016-04-13 2.9 MFS transporter in complex with inhibitor (2~{S})-3-(4-fluorophenyl)-2-[2-(3-hydroxyphenyl)ethanoylamino]-~{N}-[(1~{S})-1-phenylethyl]propanamide
5EQH 2016-04-13 2.99 MFS transporter in complex with inhibitor (2~{S})-3-(2-bromophenyl)-2-[2-(4-methoxyphenyl)ethanoylamino]-~{N}-[(1~{S})-1-phenylethyl]propanamide
5EQI 2016-04-13 3.0 MFS transporter in complex with Cytochalasin B
4PYP 2014-05-21 3.17 Crystal structure of the human glucose transporter GLUT1

Relevant UniProtKB Entries

Percent Identity Matching Chains Protein Accession Entry Name
97.4 Solute carrier family 2, facilitated glucose transporter member 1 P79365 GTR1_SHEEP
97.4 Solute carrier family 2, facilitated glucose transporter member 1 P11167 GTR1_RAT
97.2 Solute carrier family 2, facilitated glucose transporter member 1 P20303 GTR1_PIG
97.6 Solute carrier family 2, facilitated glucose transporter member 1 P27674 GTR1_BOVIN
97.6 Solute carrier family 2, facilitated glucose transporter member 1 P17809 GTR1_MOUSE
96.7 Solute carrier family 2, facilitated glucose transporter member 1 P13355 GTR1_RABIT
100.0 Solute carrier family 2, facilitated glucose transporter member 1 P11166 GTR1_HUMAN