Yukl Erik T, Jensen Lyndal M R, Davidson Victor L, Wilmot Carrie M
Department of Biochemistry, Molecular Biology and Biophysics, University of Minnesota, 321 Church Street SE, Minneapolis, MN 55455, USA.
Acta Crystallogr Sect F Struct Biol Cryst Commun. 2013 Jul;69(Pt 7):738-43. doi: 10.1107/S1744309113016539. Epub 2013 Jun 27.
MauG has been cocrystallized with methylamine dehydrogenase (MADH) with its TTQ cofactor in the o-quinol (TTQOQ) and quinone (TTQOX) forms and the structures of the resulting complexes have been solved. The TTQOQ structure crystallized in either space group P21 or C2, while the TTQOX 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.
MauG已与甲基胺脱氢酶（MADH）共结晶，其TTQ辅因子呈邻醌（TTQOQ）和醌（TTQOX）形式，并且已解析出所得复合物的结构。TTQOQ结构在空间群P21或C2中结晶，而TTQOX结构在空间群P1中结晶。之前解析出的MauG与带有未完全形成的TTQ辅因子的MADH（preMADH）复合物的结构也在空间群P1中结晶，尽管晶胞参数不同。尽管晶体形式有所变化，但结构实际上是相同的，仅在蛋白质-蛋白质界面处有非常微小的变化。讨论了这些结构与所测得的MauG和各种形式的MADH之间亲和力变化的相关性。
