Structural and functional characterization of a novel type-III dockerin from Ruminococcus flavefaciens.

Autor: Karpol A; Department of Biological Chemistry, The Weizmann Institute of Science, Rehovot 76100, Israel., Jobby MK, Slutzki M, Noach I, Chitayat S, Smith SP, Bayer EA
Jazyk: angličtina
Zdroj: FEBS letters [FEBS Lett] 2013 Jan 04; Vol. 587 (1), pp. 30-6. Date of Electronic Publication: 2012 Nov 27.
DOI: 10.1016/j.febslet.2012.11.012
Abstrakt: Phylogenetic analysis of known dockerins in Ruminococcus flavefaciens revealed a novel subtype, type-III, in the scaffoldin proteins, ScaA, ScaB, ScaC and ScaE. In this study, we explored the Ca²⁺-binding properties of the type-III dockerin from the ScaA scaffoldin (ScaADoc) using a battery of structural and biophysical approaches including circular dichroism spectroscopy, isothermal titration calorimetry, differential scanning calorimetry, and nuclear magnetic resonance spectroscopy. Despite the lack of a second canonical Ca²⁺-binding loop, the behaviour of ScaADoc is similar with respect to other dockerin protein modules in terms of its responsiveness to Ca²⁺ and affinity for the cohesin from the ScaB scaffoldin. Our results highlight the robustness of dockerin modules and how their Ca²⁺-binding properties can be exploited in the construction of designer cellulosomes.
(Copyright © 2012 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.)
Databáze: MEDLINE
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