AbstractThe chaperonin GroEL contains two seven-subunit rings, and allosteric signals between them are required to complete the GroEL reaction cycle. For this reason SR1, a mutant of GroEL that forms only single rings, cannot function as a chaperone. Mutations in SR1 that restore chaperone function weaken its interaction with the cochaperonin GroES. We predicted that GroES mutants with reduced affinity for GroEL would also restore function to SR1. To test this, we mutated residues in GroES in and near its contact site with GroEL. Nearly half of the mutants showed partial function with SR1. Two mutants were confirmed to have reduced affinity for GroEL. Intriguingly, some GroES mutants were able to function with active single ring mutants of ...
<p>For simplicity, only one ring of the GroEL 14-mer is shown. In wild type GroEL (<i>upper</i>), th...
AbstractGroEL/S chaperonin ring complexes fold many unrelated proteins. To understand the basis and ...
The chaperonin GroEL is a large complex composed of 14 identical 57-kDa subunits that requires ATP a...
AbstractThe chaperonin GroEL contains two seven-subunit rings, and allosteric signals between them a...
The mechanism of GroEL (chaperonin)-mediated protein folding is only partially understood. We have a...
chaperonin GroEL subunit consists of three domains linked via two hinge regions, and each domain is...
The bacterial chaperonin GroEL and its cofactor, GroES, form a nano-cage for a single molecule of su...
An interesting example of an allosteric protein is the chaperonin GroEL. It undergoes adenosine 5'-t...
We studied the interaction between GroES and a single-ring mutant (SR1) of GroEL by the NMR titratio...
The chaperonin GroEL adopts a double-ring structure with various modes of allosteric communication. ...
The GroES and GroEL proteins of Escherichia coli function together as the GroE molecular chaperone m...
The 2.9A resolution crystal structure of apo wild-type GroEL was determined for the first time and r...
The productive folding of substrate proteins by the GroEL complex of Escherichia coli requires the a...
A double ring-shaped GroEL consisting of 14 ATPase subunits assists protein folding, together with c...
BACKGROUND: The Escherichia coli chaperonin GroEL subunit consists of three domains linked via two h...
<p>For simplicity, only one ring of the GroEL 14-mer is shown. In wild type GroEL (<i>upper</i>), th...
AbstractGroEL/S chaperonin ring complexes fold many unrelated proteins. To understand the basis and ...
The chaperonin GroEL is a large complex composed of 14 identical 57-kDa subunits that requires ATP a...
AbstractThe chaperonin GroEL contains two seven-subunit rings, and allosteric signals between them a...
The mechanism of GroEL (chaperonin)-mediated protein folding is only partially understood. We have a...
chaperonin GroEL subunit consists of three domains linked via two hinge regions, and each domain is...
The bacterial chaperonin GroEL and its cofactor, GroES, form a nano-cage for a single molecule of su...
An interesting example of an allosteric protein is the chaperonin GroEL. It undergoes adenosine 5'-t...
We studied the interaction between GroES and a single-ring mutant (SR1) of GroEL by the NMR titratio...
The chaperonin GroEL adopts a double-ring structure with various modes of allosteric communication. ...
The GroES and GroEL proteins of Escherichia coli function together as the GroE molecular chaperone m...
The 2.9A resolution crystal structure of apo wild-type GroEL was determined for the first time and r...
The productive folding of substrate proteins by the GroEL complex of Escherichia coli requires the a...
A double ring-shaped GroEL consisting of 14 ATPase subunits assists protein folding, together with c...
BACKGROUND: The Escherichia coli chaperonin GroEL subunit consists of three domains linked via two h...
<p>For simplicity, only one ring of the GroEL 14-mer is shown. In wild type GroEL (<i>upper</i>), th...
AbstractGroEL/S chaperonin ring complexes fold many unrelated proteins. To understand the basis and ...
The chaperonin GroEL is a large complex composed of 14 identical 57-kDa subunits that requires ATP a...