Cloned (Comment) | Organism |
---|---|
expression in Escherichia coli | Synechocystis sp. |
Crystallization (Comment) | Organism |
---|---|
in complex with S-adenosylmethionine and S-adenosylhomocysteine at resolutions of 1.6 and 1.7 A, respectively. Conformational changes of the two arm regions may modulate binding and release of substrates/products to and from the active site. Residues Tyr28 and His 139 play essential roles for methyl transfer reaction but are not indispensable for cofactor/substrate binding | Synechocystis sp. |
Protein Variants | Comment | Organism |
---|---|---|
H139A | loss of more than 80% of methyltransferase activity, mutant has comparable Kd values for Mg-phosphate as the wild type protein | Synechocystis sp. |
H139N | loss of more than 80% of methyltransferase activity, mutant has comparable Kd values for Mg-phosphate as the wild type protein | Synechocystis sp. |
H139Q | loss of more than 80% of methyltransferase activity, mutant has comparable Kd values for Mg-phosphate as the wild type protein | Synechocystis sp. |
Y28A | loss of more than 80% of methyltransferase activity, mutant has comparable Kd values for Mg-phosphate as the wild type protein | Synechocystis sp. |
Y28F | mutation leads to inclusion body formation during bacterial expression | Synechocystis sp. |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Synechocystis sp. | Q55467 | - |
- |
Synonyms | Comment | Organism |
---|---|---|
ChlM | - |
Synechocystis sp. |