NDLI: The effect of calciums on molecular motions of proteinase K

Content Provider	Springer Nature Link
Author	Liu, Shu Qun Tao, Yan Meng, Zhao Hui Fu, Yun Xin Zhang, Ke Qin
Copyright Year	2010
Abstract	The native serine protease proteinase K binds two calcium cations. It has been reported that Ca2+ removal decreased the enzyme’s thermal stability and to some extent the substrate affinity, but has discrepant effects on catalytic activity of the enzyme. Molecular dynamics simulations were performed on the Ca2+-bound and Ca2+-free proteases to investigate the mechanism by which the calciums affect the structural stability, molecular motions, and catalytic activity of proteinase K. Very similar structural properties were observed between these two forms of proteinase K during simulations; and several long-lived hydrogen bonds and salt bridges common to both forms of proteinase K were found to be crucial in maintaining the local conformations around these two Ca2+ sites. Although Ca2+ removal enhanced the overall flexibility of proteinase K, the flexibility in a limited number of segments surrounding the substrate-binding pockets decreased. The largest differences in the equilibrium structures of the two simulations indicate that, upon the removal of Ca2+, the large concerted motion originating from the Ca1 site can transmit to the substrate-binding regions but not to the catalytic triad residues. In conjunction with the large overlap of the essential subspaces between the two simulations, these results not only provide insight into the dynamics of the underlying molecular mechanism responsible for the unchanged enzymatic activity as well as the decreased thermal stability and substrate affinity of proteinase K upon Ca2+ removal, but also complement the experimentally determined structural and biochemical data.
Starting Page	289
Ending Page	300
Page Count	12
File Format	PDF
ISSN	16102940
Journal	Journal of Molecular Modeling
Volume Number	17
Issue Number	2
e-ISSN	09485023
Language	English
Publisher	Springer-Verlag
Publisher Date	2010-05-06
Publisher Place	Berlin, Heidelberg
Access Restriction	One Nation One Subscription (ONOS)
Subject Keyword	Calcium Catalytic activity Essential dynamics Large concerted motions Molecular dynamics Proteinase K Structural stability Computer Application in Life Sciences Life Sciences Health Informatics Molecular Medicine Biomedicine general Computer Applications in Chemistry
Content Type	Text
Resource Type	Article
Subject	Organic Chemistry Physical and Theoretical Chemistry Computational Theory and Mathematics Catalysis Inorganic Chemistry Computer Science Applications

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