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Pustelny, K.* ; Zdzalik, M.* ; Stach, N.* ; Stec-Niemczyk, J.* ; Cichon, P.* ; Czarna, A.* ; Popowicz, G.M. ; Mak, P.* ; Dra̧g, M.* ; Salvesen, G.S.* ; Władyka, B.* ; Potempa, J.S.* ; Dubin, A.* ; Dubin, G.*

Staphylococcal SplB serine protease utilizes a novel molecular mechanism of activation.

J. Biol. Chem. 289, 15544-15553 (2014)
DOI
Open Access Green as soon as Postprint is submitted to ZB.
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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Publication type Article: Journal article
Document type Scientific Article
Corresponding Author
Keywords 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
Journal Journal of Biological Chemistry, The
Quellenangaben Volume: 289, Issue: 22, Pages: 15544-15553 Article Number: , Supplement: ,
Publisher American Society for Biochemistry and Molecular Biology
Publishing Place Bethesda
Non-patent literature Publications
Reviewing status Peer reviewed
Institute(s) Institute of Structural Biology (STB)