Premium
Crystal structure of AibC, a reductase involved in alternative de novo isovaleryl coenzyme A biosynthesis in Myxococcus xanthus
Author(s) -
Bock Tobias,
Müller Rolf,
Blankenfeldt Wulf
Publication year - 2016
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.572
H-Index - 37
ISSN - 2053-230X
DOI - 10.1107/s2053230x16011146
Subject(s) - myxococcus xanthus , myxobacteria , biosynthesis , reductase , cofactor , stereochemistry , oxidoreductase , biochemistry , biology , enzyme , chemistry , bacteria , gene , genetics , mutant
Isovaleryl coenzyme A (IV‐CoA) performs a crucial role during development and fruiting‐body formation in myxobacteria, which is reflected in the existence of a de novo biosynthetic pathway that is highly upregulated when leucine, the common precursor of IV‐CoA, is limited. The final step in de novo IV‐CoA biosynthesis is catalyzed by AibC, a medium‐chain dehydrogenase/reductase. Here, the crystal structure of AibC from Myxococcus xanthus refined to 2.55 Å resolution is presented. The protein adopts two different conformations in the crystal lattice, which is a consequence of partial interaction with the purification tag. Based on this structure, it is suggested that AibC most probably uses a Zn 2+ ‐supported catalytic mechanism in which NADPH is preferred over NADH. Taken together, this study reveals structural details of the alternative IV‐CoA‐producing pathway in myxobacteria, which may serve as a base for further biotechnological research and biofuel production.