Literature summary for 2.1.1.37 extracted from

Konarev, P.V.; Kachalova, G.S.; Ryazanova, A.Y.; Kubareva, E.A.; Karyagina, A.S.; Bartunik, H.D.; Svergun, D.I.
Flexibility of the linker between the domains of DNA methyltransferase SsoII revealed by small-angle X-ray scattering: implications for transcription regulation in SsoII restriction-modification system (2014), PLoS ONE, 9, e93453.

Cloned(Commentary)

Cloned (Comment)	Organism
-	Shigella sonnei

Crystallization (Commentary)

Crystallization (Comment)	Organism
small-angle X-ray scattering reveals two distinct protein domains of unequal size. The larger domain matches the crystallographic structure of DNA methyltransferase HhaI, and the cleft in this domain is occupied by DNA in the model. Homology modeling represents the N-terminal region either as a flexible chain of dummy residues or as a rigid structure of a homologous protein connected to the methyltransferase domain by a short flexible linker. Both models demonstrate high mobility of the N-terminal region	Shigella sonnei

Crystallization (Comment)

Organism

small-angle X-ray scattering reveals two distinct protein domains of unequal size. The larger domain matches the crystallographic structure of DNA methyltransferase HhaI, and the cleft in this domain is occupied by DNA in the model. Homology modeling represents the N-terminal region either as a flexible chain of dummy residues or as a rigid structure of a homologous protein connected to the methyltransferase domain by a short flexible linker. Both models demonstrate high mobility of the N-terminal region

Shigella sonnei

Organism

Organism	UniProt	Comment	Textmining
Shigella sonnei	P34879	-	-

Synonyms

Synonyms	Comment	Organism
M.SsoII	-	Shigella sonnei
ssoIIM	-	Shigella sonnei

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Release 2023.1 (January 2023)