title: Influence of key amino acid mutation on the active site structure and on folding in acetyl-CoA synthase: a theoretical perspective.
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.
authors.affiliation: 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.
authors.forename: Claudio
authors.initials: C
authors.lastname: Greco
authors.forename: Antonella
authors.initials: A
authors.lastname: Ciancetta
authors.forename: Maurizio
authors.initials: M
authors.lastname: Bruschi
authors.forename: Alexander
authors.initials: A
authors.lastname: Kulesza
authors.forename: Giorgio
authors.initials: G
authors.lastname: Moro
authors.forename: Ugo
authors.initials: U
authors.lastname: Cosentino
mesh_terms: D000106:Acetate-CoA Ligase / Q000737:chemistry*; D000445:Aldehyde Oxidoreductases / Q000737:chemistry*; D020134:Catalytic Domain; D003545:Cysteine / Q000737:chemistry*; D006639:Histidine / Q000737:chemistry*; D008958:Models, Molecular; D009097:Multienzyme Complexes / Q000737:chemistry*; D009154:Mutation; D017510:Protein Folding
chemical_list: D009097:Multienzyme Complexes; D006639:Histidine; D000445:Aldehyde Oxidoreductases; C019823:carbon monoxide dehydrogenase; D000106:Acetate-CoA Ligase; D003545:Cysteine