Protein recognition of ammonium cations using side-chain aromatics: a structural variation for secondary ammonium ligands.
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.
Raine
A R
AR
Department of Biochemistry, University of Cambridge, United Kingdom.
Yang
C C
CC
Packman
L C
LC
White
S A
SA
Mathews
F S
FS
Scrutton
N S
NS
D001665:Binding Sites; D002412:Cations; D003460:Crystallization; D006860:Hydrogen Bonding; D008958:Models, Molecular; D010089:Oxidoreductases, N-Demethylating / Q000737:chemistry* / Q000378:metabolism; D000644:Quaternary Ammonium Compounds / Q000378:metabolism*
D002412:Cations; D000644:Quaternary Ammonium Compounds; D010089:Oxidoreductases, N-Demethylating; C020064:dimethylamine dehydrogenase