Title

Structures of MauG in complex with quinol and quinone MADH

Authors

Authors

E. T. Yukl; L. M. R. Jensen; V. L. Davidson;C. M. Wilmot

Comments

Authors: contact us about adding a copy of your work at STARS@ucf.edu

Abbreviated Journal Title

Acta Crystallogr. F-Struct. Biol. Cryst. Commun.

Keywords

TRYPTOPHAN TRYPTOPHYLQUINONE BIOSYNTHESIS; METHYLAMINE DEHYDROGENASE; PARACOCCUS-DENITRIFICANS; INTERMEDIATE; BIOGENESIS; COFACTOR; COOT; Biochemical Research Methods; Biochemistry & Molecular Biology; Biophysics; Crystallography

Abstract

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.

Journal Title

Acta Crystallographica Section F-Structural Biology and Crystallization Communications

Volume

69

Publication Date

1-1-2013

Document Type

Article

Language

English

First Page

738

Last Page

743

WOS Identifier

WOS:000321427900007

ISSN

1744-3091

Share

COinS