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Papaleo E, Parravicini F, Grandori R, et al. Structural investigation of the cold-adapted acylaminoacyl peptidase from Sporosarcina psychrophila by atomistic simulations and biophysical methods. Biochim Biophys Acta. 2014;1844(12):2203-13doi: 10.1016/j.bbapap.2014.09.018.
Papaleo, E., Parravicini, F., Grandori, R., De Gioia, L., & Brocca, S. (2014). Structural investigation of the cold-adapted acylaminoacyl peptidase from Sporosarcina psychrophila by atomistic simulations and biophysical methods. Biochimica et biophysica acta, 1844(12), 2203-13. https://doi.org/10.1016/j.bbapap.2014.09.018
Papaleo, Elena, et al. "Structural investigation of the cold-adapted acylaminoacyl peptidase from Sporosarcina psychrophila by atomistic simulations and biophysical methods." Biochimica et biophysica acta vol. 1844,12 (2014): 2203-13. doi: https://doi.org/10.1016/j.bbapap.2014.09.018
Papaleo E, Parravicini F, Grandori R, De Gioia L, Brocca S. Structural investigation of the cold-adapted acylaminoacyl peptidase from Sporosarcina psychrophila by atomistic simulations and biophysical methods. Biochim Biophys Acta. 2014 Dec;1844(12):2203-13. doi: 10.1016/j.bbapap.2014.09.018. Epub 2014 Oct 01. PMID: 25280393.
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Biochim Biophys Acta. 2014 Dec;1844(12):2203-13. doi: 10.1016/j.bbapap.2014.09.018. Epub 2014 Oct 01.

Structural investigation of the cold-adapted acylaminoacyl peptidase from Sporosarcina psychrophila by atomistic simulations and biophysical methods.

Biochimica et biophysica acta

Elena Papaleo, Federica Parravicini, Rita Grandori, Luca De Gioia, Stefania Brocca

Affiliations

  1. Department of Biotechnology and Biosciences, University of Milano-Bicocca, 20126, Milan, Italy. Electronic address: [email protected].
  2. Department of Biotechnology and Biosciences, University of Milano-Bicocca, 20126, Milan, Italy.

PMID: 25280393 DOI: 10.1016/j.bbapap.2014.09.018

Abstract

Protein structure and dynamics are crucial for protein function. Thus, the study of conformational properties can be very informative for characterizing new proteins and to rationalize how residue substitutions at specific protein sites affect its dynamics, activity and thermal stability. Here, we investigate the structure and dynamics of the recently isolated cold-adapted acylaminoacyl peptidase from Sporosarcina psychrophila (SpAAP) by the integration of simulations, circular dichroism, mass spectrometry and other experimental data. Our study notes traits of cold-adaptation, such as lysine-to-arginine substitutions and a lack of disulphide bridges. Cold-adapted enzymes are generally characterized by a higher number of glycine residues with respect to their warm-adapted counterparts. Conversely, the SpAAP glycine content is lower than that in the warm-adapted variants. Nevertheless, glycine residues are strategically located in proximity to the functional sites in SpAAP, such as the active site and the linker between the two domains.. In particular, G457 reduces the steric hindrance around the nucleophile elbow. Our results suggest a local weakening of the intramolecular interactions in the cold-adapted enzyme. This study offers a basis for the experimental mutagenesis of SpAAP and related enzymes. The approaches employed in this study may also provide a more general framework to characterize new protein structures in the absence of X-ray or NMR data.

Copyright © 2014 Elsevier B.V. All rights reserved.

Keywords: Acylaminoacyl peptidase; Acylpeptide hydrolase; Molecular dynamics; Psychrophilic enzyme; Three-dimensional structure; beta-Barrel

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