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Crystal Structure of an Intracellular Subtilisin Reveals Novel Structural Features Unique to this Subtilisin Family

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JournalStructure
DatePublished - 9 Jun 2010
Issue number6
Volume18
Number of pages12
Pages (from-to)744-755
Original languageEnglish

Abstract

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 angstrom 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.

    Research areas

  • BACILLUS-SUBTILIS, SERINE-PROTEASE, CARBOXYL PROTEINASE, MOLECULAR-GRAPHICS, COMPLEX, INHIBITORS, PRECURSOR, SEQUENCE, CLONING, ENZYME

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