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Literature summary for 2.1.1.11 extracted from

  • Chen, X.; Wang, X.; Feng, J.; Chen, Y.; Fang, Y.; Zhao, S.; Zhao, A.; Zhang, M.; Liu, L.
    Structural insights into the catalytic mechanism of Synechocystis magnesium protoporphyrin IX O-methyltransferase (ChlM) (2014), J. Biol. Chem., 289, 25690-25698.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli Synechocystis sp.

Crystallization (Commentary)

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

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

Organism UniProt Comment Textmining
Synechocystis sp. Q55467
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Synonyms

Synonyms Comment Organism
ChlM
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Synechocystis sp.