2.1.1.179: 16S rRNA (guanine1405-N7)-methyltransferase

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For detailed information about 16S rRNA (guanine1405-N7)-methyltransferase, go to the full flat file.

Reaction

Synonyms

16S rRNA (m7G1405) methyltransferase, 16S rRNA methyltransferase, 16S rRNA N7 G1405 methyltransferase, 16S-RMTase, ArmA, FmrO, G1405 methyltransferase ArmA, GrmA, GrmB, Kmr, Krm, M7G1405 MTase, methyltransferase RmtC, methyltransferase Sgm, N7-G1405 16S-RMTase, NbrB, RmtA, RmtB, RmtC, RmtD, RmtD2, RmtF, RmtG, sgm, Sgm methyltransferase, Sgm MTase, sisomicin-gentamicin methylase, sisomicin-gentamicin methyltransferase, sisomicin-gentamicin resistance methylase, Smr1

ECTree

     2 Transferases

         2.1 Transferring one-carbon groups

             2.1.1 Methyltransferases

                2.1.1.179 16S rRNA (guanine1405-N7)-methyltransferase

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Results	in table
447	AA Sequence
12	Application
25	Cloned(Commentary)
13	Cofactor
3	Crystallization (Commentary)
41	General Information
1	Inhibitors
5	Molecular Weight [Da]
38	Natural Substrates/ Products (Substrates)
83	Organism
13	PDB ID
3	pH Optimum
40	Protein Variants
7	Purification (Commentary)
3	Reaction
43	Reference
51	Substrates and Products (Substrate)
5	Subunits
92	Synonyms
1	Systematic Name
3	Temperature Optimum [°C]
1	Temperature Stability [°C]

Crystallization

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Crystallization on EC 2.1.1.179 - 16S rRNA (guanine1405-N7)-methyltransferase

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CRYSTALLIZATION (Commentary)

ORGANISM

UNIPROT

LITERATURE

RmtB containing S-adenosyl-L-homocysteine in the active site

Escherichia coli

-

712741

purified Sgm is complexed with 5 mM of the cofactors S-adenosylmethionine/S-adenosylhomocysteine. Crystallization trials are carried out at room temperature by hanging-drop vapor-diffusion method, structure of Sgm in complex with cofactors S-adenosylmethionine and S-adenosylhomocysteine is determined at 2.0 A and 2.1 A resolution, respectively

Micromonospora zionensis

Q7M0R2

705988

in complex with S-adenosylhomocysteine. An N-terminal domain surface within RmtC, comprising basic residues from both the N1 and N2 subdomains, directly contributes to 30S-binding affinity. Additional residues lining a contiguous adjacent surface on the C-terminal domain are critical for 16S rRNA modification but do not directly contribute to the binding affinity

Proteus mirabilis

Q33DX5

757224