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Literature summary for 3.1.21.4 extracted from

  • Callahan, S.J.; Luyten, Y.A.; Gupta, Y.K.; Wilson, G.G.; Roberts, R.J.; Morgan, R.D.; Aggarwal, A.K.
    Structure of type IIL restriction-modification enzyme MmeI in complex with DNA has implications for engineering new specificities (2016), PLoS Biol., 14, e1002471.
    View publication on PubMed
Search for more literature for 3.1.21.4

Crystallization (Commentary)

Crystallization (Comment) Organism
crystal structure of MmeI in complex with its DNA substrate (a 29-mer DNA duplex containing a single MmeI recognition site (TCCGAC)) and an S-adenosylmethionine analog sinefungin. The co-crystals are obtained in the presence of sinefungin and diffracted to 2.6 A resolution with synchrotron radiation. They belong to space group P1 with unit cell dimensions of a = 61.87 A, b = 95.29 A, c = 161.96 A, alpha = 72.84°, beta = 89.15°, and gamma = 71.61°, and contain two MmeI/DNA/sinefungin complexes in the crystallographic asymmetric unit Methylophilus methylotrophus

Inhibitors

Inhibitors Comment Organism Structure
sinefungin
-
 Methylophilus methylotrophus

Organism

Organism UniProt Comment Textmining
Methylophilus methylotrophus B2MU09
-
-

Purification (Commentary)

Purification (Comment) Organism
-
 Methylophilus methylotrophus

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
DNA + H2O the enzyme is resilient to specificity changes at the first position of the recognition sequence (5'-TCCRAC-3') Methylophilus methylotrophus ?
-
 ?

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
 assay at Methylophilus methylotrophus

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.9
-
 assay at Methylophilus methylotrophus