Literature summary for 3.4.21.62 extracted from

Vevodova, J.; Gamble, M.; Kuenze, G.; Ariza, A.; Dodson, E.; Jones, D.D.; Wilson, K.S.
Crystal structure of an intracellular subtilisin reveals novel structural features unique to this subtilisin family (2010), Structure, 18, 744-755.

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Cloned(Commentary)

Cloned (Comment)	Organism
expressed in Escherichia coli	Alkalihalobacillus clausii

Crystallization (Commentary)

Crystallization (Comment)	Organism
subtilisin Carlsberg covalently bound to the inhibitor L-[(1R)-1-acetamido-2-(1-naphthyl)ethyl]boronic acid, refined at 2.65 A is used in the studies	Alkalihalobacillus clausii
the structure is determined to a resolution of 1.56 A. ISP from Bacillus clausii is dimeric, with residues from the C terminus making a major contribution to the dimer interface by crossing over to contact the partner subunit. A short N-terminal extension binds back across the active site to provide a potential novel regulatory mechanism of intrinsic proteolytic activity: a proline residue conserved throughout the ISPs introduces a kink in the polypeptide backbone that lifts the target peptide bond out of reach of the catalytic residues	Alkalihalobacillus clausii

Crystallization (Comment)

Organism

subtilisin Carlsberg covalently bound to the inhibitor L-[(1R)-1-acetamido-2-(1-naphthyl)ethyl]boronic acid, refined at 2.65 A is used in the studies

Alkalihalobacillus clausii

the structure is determined to a resolution of 1.56 A. ISP from Bacillus clausii is dimeric, with residues from the C terminus making a major contribution to the dimer interface by crossing over to contact the partner subunit. A short N-terminal extension binds back across the active site to provide a potential novel regulatory mechanism of intrinsic proteolytic activity: a proline residue conserved throughout the ISPs introduces a kink in the polypeptide backbone that lifts the target peptide bond out of reach of the catalytic residues

Alkalihalobacillus clausii

Protein Variants

Protein Variants	Comment	Organism
S250A	inactive variant	Alkalihalobacillus clausii

Inhibitors

Inhibitors	Comment	Organism	Structure
L-[(1R)-1-acetamido-2-(1-naphthyl)ethyl]boronic acid	-	Alkalihalobacillus clausii
N-acetyl-L-tryptophan amide	molecular dynamics simulations are performed with subtilisin in the presence and in the absence of an inhibitor both in hexane and in water. The inhibitor induces an open conformation of the S1 pocket that is maintained after the removal of the ligand in anhydrous, but not in aqueous, simulations. The analysis of fluctuations suggest that this behavior is caused by the decreased flexibility exhibited by subtilisin in hexane	Alkalihalobacillus clausii

Localization

Localization	Comment	Organism	GeneOntology No.	Textmining

Molecular Weight [Da]

Molecular Weight [Da]	Molecular Weight Maximum [Da]	Comment	Organism
34780	-	MALDI-TOF	Alkalihalobacillus clausii
34782	-	MALDI-TOF, 2 * 34782 Da	Alkalihalobacillus clausii
55000	-	dimer, gel filtration	Alkalihalobacillus clausii

Organism

Organism	UniProt	Comment	Textmining
Alkalihalobacillus clausii	D0AB41	-	-

Purification (Commentary)

Purification (Comment)	Organism
using Ni-NTA chromatography	Alkalihalobacillus clausii

Subunits

Subunits	Comment	Organism
dimer	MALDI-TOF, 2 * 34782 Da	Alkalihalobacillus clausii

Synonyms

Synonyms	Comment	Organism
subtilisin	-	Alkalihalobacillus clausii
subtilisin A	-	Alkalihalobacillus clausii