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Literature summary for 3.1.21.4 extracted from

  • Shen, B.W.; Doyle, L.; Bradley, P.; Heiter, D.F.; Lunnen, K.D.; Wilson, G.G.; Stoddard, B.L.
    Structure, subunit organization and behavior of the asymmetric Type IIT restriction endonuclease BbvCI (2019), Nucleic Acids Res., 47, 450-467 .
    View publication on PubMedView publication on EuropePMC
Search for more literature for 3.1.21.4

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli Brevibacillus brevis

Crystallization (Commentary)

Crystallization (Comment) Organism
crystallization of the R2 subunit at low pH reveals an elongated dimer with the two catalytic sites located on opposite sides. Subsequent crystallization at physiological pH reveals a tetramer comprising two copies of each subunit, with a pair of deep clefts each containing two catalytic sites appropriately positioned and oriented for DNA cleavage Brevibacillus brevis

Protein Variants

Protein Variants Comment Organism
D140A no detectable activity in dsDNA nicking, mutant R1 subunit/wild-type R2 subunit Brevibacillus brevis
D140A/E167A/K169A no detectable activity in dsDNA nicking, mutant R1 subunit/wild-type R2 subunit Brevibacillus brevis
D144A no detectable activity in ssDNA nicking, mutant R2 subunit/wild-type R1 subunit Brevibacillus brevis
D146A no detectable activity in dsDNA nicking, mutant R2 subunit/wild-type R1 subunit Brevibacillus brevis
D146A/E177A slight detectable activity in dsDNA nicking, mutant R2 subunit/wild-type R1 subunit Brevibacillus brevis
D146A/E177A/K179A no detectable activity in dsDNA nicking, mutant R2 subunit/wild-type R1 subunit Brevibacillus brevis
D149A no detectable activity in ssDNA nicking, mutant R1 subunit/wild-type R2 subunit Brevibacillus brevis
D226A no detectable activity in ssDNA nicking, mutant R2 subunit/wild-type R1 subunit Brevibacillus brevis
E139A no detectable activity in ssDNA nicking, mutant R1 subunit/wild-type R2 subunit Brevibacillus brevis
E147A no detectable activity in ssDNA nicking, mutant R1 subunit/wild-type R2 subunit Brevibacillus brevis
E155A no detectable activity in ssDNA nicking, low activity in dsDNA nicking, mutant R1 subunit/wild-type R2 subunit Brevibacillus brevis
E163A no detectable activity in ssDNA nicking, mutant R2 subunit/wild-type R1 subunit Brevibacillus brevis
E165A no detectable activity in ssDNA nicking, mutant R2 subunit/wild-type R1 subunit Brevibacillus brevis
E167A slight activity in dsDNA nicking, mutant R1 subunit/wild-type R2 subunit Brevibacillus brevis
E167A/K169A no detectable activity in dsDNA nicking, mutant R1 subunit/wild-type R2 subunit Brevibacillus brevis
E167G slight activity in dsDNA nicking, mutant R1 subunit/wild-type R2 subunit Brevibacillus brevis
E177A slight activity in dsDNA nicking, mutant R2 subunit/wild-type R1 subunit Brevibacillus brevis
E177G no detectable activity in dsDNA nicking, mutant R2 subunit/wild-type R1 subunit Brevibacillus brevis
E201A no detectable activity in ssDNA nicking, mutant R1 subunit/wild-type R2 subunit Brevibacillus brevis
E211A no detectable activity in dsDNA nicking and no detectable activity in ssDNA nicking, mutant R2 subunit/wild-type R1 subunit Brevibacillus brevis
E218A no detectable activity in ssDNA nicking, no activity in dsDNA nicking, mutant R1 subunit/wild-type R2 subunit Brevibacillus brevis
E227A no detectable activity in dsDNA nicking and no detectable activity in ssDNA nicking, mutant R2 subunit/wild-type R1 subunit Brevibacillus brevis
E95A no detectable activity in ssDNA and in dsDNA nicking, mutant R1 subunit/wild-type R2 subunit Brevibacillus brevis
K169A low activity in dsDNA nicking, mutant R1 subunit/wild-type R2 subunit Brevibacillus brevis
K179A no detectable activity in dsDNA nicking, mutant R2 subunit/wild-type R1 subunit Brevibacillus brevis
N138A no detectable activity in ssDNA nicking, mutant R1 subunit/wild-type R2 subunit Brevibacillus brevis

Organism

Organism UniProt Comment Textmining
Brevibacillus brevis Q5D6Y5 AND Q5D6Y4 Q5D6Y5: endonuclease subunit R1, Q5D6Y4: endonuclease subunit R2
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
double-stranded DNA + H2O the enzyme recognizes and cleaves the seven base pair sequence 5'-CCTCAGC-3', generating 3-base, 5'-overhangs Brevibacillus brevis double-stranded DNA fragments with 3-base 5'-overhangs
-
 ?

Subunits

Subunits Comment Organism
dimer the enzyme exists in a dynamic equilibrium between dimeric, tetrameric, and perhaps larger assemblages. BbvCI is composed of two protein subunits (R1 and R2), each containing one catalytic site. Crystallization of the R2 subunit at low pH reveals an elongated dimer with the two catalytic sites located on opposite sides. Subsequent crystallization at physiological pH reveals a tetramer comprising two copies of each subunit, with a pair of deep clefts each containing two catalytic sites appropriately positioned and oriented for DNA cleavage Brevibacillus brevis
tetramer the enzyme exists in a dynamic equilibrium between dimeric, tetrameric, and perhaps larger assemblages. BbvCI is composed of two protein subunits (R1 and R2), each containing one catalytic site. Crystallization of the R2 subunit at low pH reveals an elongated dimer with the two catalytic sites located on opposite sides. Subsequent crystallization at physiological pH reveals a tetramer comprising two copies of each subunit, with a pair of deep clefts each containing two catalytic sites appropriately positioned and oriented for DNA cleavage Brevibacillus brevis

Synonyms

Synonyms Comment Organism
type IIT restriction endonuclease BbvCI
-
 Brevibacillus brevis