EC Number | Crystallization (Comment) | Organism |
---|---|---|
1.8.4.11 | structure of dimeric MsrA to 2.9 A resolution, having the dimer interface around the two catalytic Cys16 residues. A central cone-shaped hole is present in the surface model of dimeric structure, and the two Cys16 residues constitute the base of the hole | Alkaliphilus oremlandii |
EC Number | Protein Variants | Comment | Organism |
---|---|---|---|
1.8.4.11 | E55A | almost completely inactive, dimerization is hardly detectable | Alkaliphilus oremlandii |
1.8.4.11 | E55D | almost completely inactive, incapable of dimerization | Alkaliphilus oremlandii |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
1.8.4.11 | Alkaliphilus oremlandii | A8MI53 | - |
- |
1.8.4.11 | Alkaliphilus oremlandii OhILAs | A8MI53 | - |
- |
EC Number | Subunits | Comment | Organism |
---|---|---|---|
1.8.4.11 | dimer | and monomer. Monomeric CoMsrA dimerizes in the presence of its substrate methionine sulfoxide via an intermolecular disulfide bond between catalytic Cys16 residues. The dimeric MsrA is resolved by the reductant glutaredoxin | Alkaliphilus oremlandii |
1.8.4.11 | monomer | and dimer. monomeric CoMsrA dimerizes in the presence of its substrate methionine sulfoxide via an intermolecular disulfide bond between catalytic Cys16 residues. The dimeric MsrA is resolved by the reductant glutaredoxin | Alkaliphilus oremlandii |