Structures of MauG in complex with quinol and quinone MADH
Abbreviated Journal Title
Acta Crystallogr. F-Struct. Biol. Cryst. Commun.
TRYPTOPHAN TRYPTOPHYLQUINONE BIOSYNTHESIS; METHYLAMINE DEHYDROGENASE; PARACOCCUS-DENITRIFICANS; INTERMEDIATE; BIOGENESIS; COFACTOR; COOT; Biochemical Research Methods; Biochemistry & Molecular Biology; Biophysics; Crystallography
MauG has been cocrystallized with methylamine dehydrogenase (MADH) with its TTQ cofactor in the o-quinol (TTQ(OQ)) and quinone (TTQ(OX)) forms and the structures of the resulting complexes have been solved. The TTQ(OQ) structure crystallized in either space group P2(1) or C2, while the TTQ(OX) structure crystallized in space group P1. The previously solved structure of MauG in complex with MADH bearing an incompletely formed TTQ cofactor (preMADH) also crystallized in space group P1, although with different unit-cell parameters. Despite the changes in crystal form, the structures are virtually identical, with only very minor changes at the protein-protein interface. The relevance of these structures with respect to the measured changes in affinity between MauG and various forms of MADH is discussed.
Acta Crystallographica Section F-Structural Biology and Crystallization Communications
"Structures of MauG in complex with quinol and quinone MADH" (2013). Faculty Bibliography 2010s. 4913.