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Open Access Gold möglich sobald Verlagsversion bei der ZB eingereicht worden ist.
Staphylococcal SplB serine protease utilizes a novel molecular mechanism of activation.
J. Biol. Chem. 289, 15544-15553 (2014)
Background: Activation of SplB protease requires precise N-terminal processing, but the molecular mechanism remains unknown. Results: The new N-terminal Glu-1 forms a distinctive H-bond network essential for full catalytic activity. Conclusion: Changes in protein dynamics rather than a direct effect on the active site are of crucial importance in SplB activation. Significance: A novel serine protease activation mechanism was uncovered.
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Publikationstyp
Artikel: Journalartikel
Dokumenttyp
Wissenschaftlicher Artikel
Schlagwörter
Crystal Structure ; Enzyme Inactivation ; Protease ; Serine Protease ; Staphylococcus Aureus ; Signal Peptide ; Zymogen Activation; Proteolytic-enzymes; Enzymatic-activity; Crystal-structures; Aureus; Chymotrypsinogen; Metalloprotease; Specificity; Inhibition; Refinement; Propeptide
ISSN (print) / ISBN
0021-9258
e-ISSN
1083-351X
Zeitschrift
Journal of Biological Chemistry, The
Quellenangaben
Band: 289,
Heft: 22,
Seiten: 15544-15553
Verlag
American Society for Biochemistry and Molecular Biology
Verlagsort
Bethesda
Begutachtungsstatus
Peer reviewed
Institut(e)
Institute of Structural Biology (STB)