Literature summary for 2.1.1.198 extracted from

Zhao, M.; Zhang, H.; Liu, G.; Wang, L.; Wang, J.; Gao, Z.; Dong, Y.; Zhang, L.; Gong, Y.
Structural insights into the methylation of C1402 in 16S rRNA by methyltransferase RsmI (2016), PLoS ONE, 11, e0163816 .

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Crystallization (Commentary)

Crystallization (Comment)	Organism
structure in complex with cofactor SAM, to 2.2 A resolution. RsmI consists of an N-terminal putative RNA-binding domain and a C-terminal catalytic domain with a Rossmann-like fold, and belongs to the class III MTase family. SAM is specifically bound into a negatively charged deep pocket formed by both domains by making extensive contacts. Residues Asp100 and Ala124 are vital for SAM-binding. A base-flipping mechanism of the substrate RNA is possible	Escherichia coli

Crystallization (Comment)

Organism

structure in complex with cofactor SAM, to 2.2 A resolution. RsmI consists of an N-terminal putative RNA-binding domain and a C-terminal catalytic domain with a Rossmann-like fold, and belongs to the class III MTase family. SAM is specifically bound into a negatively charged deep pocket formed by both domains by making extensive contacts. Residues Asp100 and Ala124 are vital for SAM-binding. A base-flipping mechanism of the substrate RNA is possible

Escherichia coli

Protein Variants

Protein Variants	Comment	Organism
A124L	complete loss of binding affinity, mutation abolishes the side chain-mediating H-bond with SAM	Escherichia coli
D100K	complete loss of binding affinity, mutation abolishes the side chain-mediating H-bond with SAM	Escherichia coli
F144A	binding affinities and entropy are moderately affected	Escherichia coli
Y169A	binding affinity and enthalpy/entropy are very similar to that of the wild-type	Escherichia coli

Organism

Organism	UniProt	Comment	Textmining
Escherichia coli	P67087	-	-

Synonyms

Synonyms	Comment	Organism
RsmI	-	Escherichia coli

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Release 2023.1 (January 2023)