Crystal structure of an intracellular subtilisin reveals novel structural features unique to this subtilisin family
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 o...
| Main Authors: | , , , , , , |
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| Formato: | Journal article |
| Idioma: | English |
| Publicado: |
Cell Press
2010
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| _version_ | 1826264590632091648 |
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| author | Vévodová, J Gamble, M Künze, G Ariza, A Dodson, E Jones, D Wilson, K |
| author_facet | Vévodová, J Gamble, M Künze, G Ariza, A Dodson, E Jones, D Wilson, K |
| author_sort | Vévodová, J |
| collection | OXFORD |
| description | 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 Å 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. |
| first_indexed | 2024-03-06T20:10:17Z |
| format | Journal article |
| id | oxford-uuid:2a51a97e-7775-4184-9f03-d01fd4219de8 |
| institution | University of Oxford |
| language | English |
| last_indexed | 2024-03-06T20:10:17Z |
| publishDate | 2010 |
| publisher | Cell Press |
| record_format | dspace |
| spelling | oxford-uuid:2a51a97e-7775-4184-9f03-d01fd4219de82022-03-26T12:24:21ZCrystal structure of an intracellular subtilisin reveals novel structural features unique to this subtilisin familyJournal articlehttp://purl.org/coar/resource_type/c_dcae04bcuuid:2a51a97e-7775-4184-9f03-d01fd4219de8EnglishSymplectic Elements at OxfordCell Press2010Vévodová, JGamble, MKünze, GAriza, ADodson, EJones, DWilson, KThe 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 Å 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. |
| spellingShingle | Vévodová, J Gamble, M Künze, G Ariza, A Dodson, E Jones, D Wilson, K Crystal structure of an intracellular subtilisin reveals novel structural features unique to this subtilisin family |
| title | Crystal structure of an intracellular subtilisin reveals novel structural features unique to this subtilisin family |
| title_full | Crystal structure of an intracellular subtilisin reveals novel structural features unique to this subtilisin family |
| title_fullStr | Crystal structure of an intracellular subtilisin reveals novel structural features unique to this subtilisin family |
| title_full_unstemmed | Crystal structure of an intracellular subtilisin reveals novel structural features unique to this subtilisin family |
| title_short | Crystal structure of an intracellular subtilisin reveals novel structural features unique to this subtilisin family |
| title_sort | crystal structure of an intracellular subtilisin reveals novel structural features unique to this subtilisin family |
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