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

Claudio Greco; Antonella Ciancetta; Maurizio Bruschi; Alexander Kulesza; Giorgio Moro; Ugo Cosentino

doi:10.1039/c5cc01575h

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

Chem Commun (Camb). 2015 May 18;51(40):8551-4. doi: 10.1039/c5cc01575h.

Authors

Claudio Greco¹, Antonella Ciancetta, Maurizio Bruschi, Alexander Kulesza, Giorgio Moro, Ugo Cosentino

Affiliation

¹ Department of Earth and Environmental Sciences, Milano-Bicocca University, P.zza della Scienza 1, Milan, 20126, Italy. claudio.greco@unimib.it ugo.cosentino@unimib.it.

PMID: 25896878
DOI: 10.1039/c5cc01575h

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.

Publication types

Research Support, Non-U.S. Gov't

MeSH terms

Acetate-CoA Ligase / chemistry*
Aldehyde Oxidoreductases / chemistry*
Catalytic Domain
Cysteine / chemistry*
Histidine / chemistry*
Models, Molecular*
Multienzyme Complexes / chemistry*
Mutation
Protein Folding

Substances

Multienzyme Complexes
Histidine
Aldehyde Oxidoreductases
carbon monoxide dehydrogenase
Acetate-CoA Ligase
Cysteine