Issue 40, 2015
From the journal:

Chemical Communications

Influence of key amino acid mutation on the active site structure and on folding in acetyl-CoA synthase: a theoretical perspective†

Claudio Greco,*a   Antonella Ciancetta,b   Maurizio Bruschi,a   Alexander Kulesza,a   Giorgio Moroc  and  Ugo Cosentino*a  

* Corresponding authors

a Department of Earth and Environmental Sciences, Milano-Bicocca University, P.zza della Scienza 1, Milan, Italy
E-mail: claudio.greco@unimib.it, ugo.cosentino@unimib.it
Tel: +39-02-6448-2098/2822

b Department of Pharmaceutical and Pharmacological Sciences, University of Padova, Via Marzolo 5, Padova, Italy

c Department of Biotechnology and Biosciences, Milano-Bicocca University, P.zza della Scienza 2, Milan, Italy

Abstract

Ad hoc quantum chemical modeling of the acetyl-CoA synthase local structure and folding allowed us to identify an unprecedented coordination mode of histidine sidechain to protein-embedded metal ions.

Graphical abstract: Influence of key amino acid mutation on the active site structure and on folding in acetyl-CoA synthase: a theoretical perspective

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Article information

DOI
https://doi.org/10.1039/C5CC01575H
Article type
Communication
Submitted
21 Feb 2015
Accepted
07 Apr 2015
First published
07 Apr 2015

Chem. Commun., 2015,51, 8551-8554

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Influence of key amino acid mutation on the active site structure and on folding in acetyl-CoA synthase: a theoretical perspective

C. Greco, A. Ciancetta, M. Bruschi, A. Kulesza, G. Moro and U. Cosentino, Chem. Commun., 2015, 51, 8551 DOI: 10.1039/C5CC01575H

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