Protein recognition of ammonium cations using side-chain aromatics: a structural variation for secondary ammonium ligands.

TitleProtein recognition of ammonium cations using side-chain aromatics: a structural variation for secondary ammonium ligands.
Publication TypeJournal Article
Year of Publication1995
AuthorsRaine, AR, Yang, CC, Packman, LC, White, SA, Mathews, FS, Scrutton, NS
JournalProtein Sci
Volume4
Issue12
Pagination2625-8
Date Published1995 Dec
ISSN0961-8368
KeywordsBinding Sites, Cations, Crystallization, Hydrogen Bonding, Models, Molecular, Oxidoreductases, N-Demethylating, Quaternary Ammonium Compounds
Abstract

A model for the structure of dimethylamine dehydrogenase was generated using the crystal coordinates of trimethylamine dehydrogenase. Substrate is bound in trimethylamine dehydrogenase by cation-pi bonding, but modeling of dimethylamine dehydrogenase suggests that secondary amines are bound by a mixture of cation-pi and conventional hydrogen bonding. In dimethylamine dehydrogenase, binding is orientationally more specific and distinct from those proteins that bind tertiary and quaternary amine groups.

DOI10.1002/pro.5560041222
Alternate JournalProtein Sci.
Citation Key10.1002/pro.5560041222
PubMed ID8580856
PubMed Central IDPMC2143047