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PDBsum entry 2x8j
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Contents |
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* Residue conservation analysis
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PDB id:
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Hydrolase
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Title:
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Intracellular subtilisin precursor from b. Clausii
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Structure:
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Intracellular subtilisin protease. Chain: a, c, d, e, f. Synonym: intracellular subtilisin. Engineered: yes. Mutation: yes. Other_details: these chains contain 1 oxidised cys. Intracellular subtilisin protease. Chain: b. Synonym: intracellular subtilisin.
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Source:
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Bacillus clausii. Organism_taxid: 79880. Expressed in: escherichia coli bl21. Expression_system_taxid: 511693. Other_details: isolated from a novozymes strain b. Clausii strain - strain number available on request.. Strain number available on request.
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Resolution:
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1.56Å
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R-factor:
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0.190
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R-free:
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0.230
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Authors:
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J.Vedodova,M.Gamble,A.Ariza,E.Dodson,D.D.Jones,K.S.Wilson
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Key ref:
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J.Vévodová
et al.
(2010).
Crystal structure of an intracellular subtilisin reveals novel structural features unique to this subtilisin family.
Structure,
18,
744-755.
PubMed id:
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Date:
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09-Mar-10
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Release date:
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11-Aug-10
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PROCHECK
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Headers
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References
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D0AB41
(D0AB41_ALKCL) -
Intracellular subtilisin protease from Alkalihalobacillus clausii
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Seq:
Struc:
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321 a.a.
303 a.a.*
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Key: |
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PfamA domain |
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Secondary structure |
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CATH domain |
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*
PDB and UniProt seqs differ
at 2 residue positions (black
crosses)
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Enzyme class:
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E.C.3.4.21.62
- subtilisin.
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Reaction:
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Hydrolysis of proteins with broad specificity for peptide bonds, and a preference for a large uncharged residue in P1. Hydrolyzes peptide amides.
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Structure
18:744-755
(2010)
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PubMed id:
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Crystal structure of an intracellular subtilisin reveals novel structural features unique to this subtilisin family.
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J.Vévodová,
M.Gamble,
G.Künze,
A.Ariza,
E.Dodson,
D.D.Jones,
K.S.Wilson.
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ABSTRACT
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The intracellular subtilisin proteases (ISPs) are the only known members of the
important and ubiquitous subtilisin family that function exclusively within the
cell, constituting a major component of the degradome in many Gram-positive
bacteria. The first ISP structure reported herein at a spacing of 1.56 A reveals
features unique among subtilisins that has enabled potential functional and
physiological roles to be assigned to sequence elements exclusive to the ISPs.
Unlike all other subtilisins, ISP from B. 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.
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Links
