Crystal structure of AibC, a reductase involved in alternative de novo isovaleryl coenzyme A biosynthesis in Myxococcus xanthus. Issue 8 (4th August 2016)

• Record Type: Journal Article
• Authors: Bock, Tobias; Müller, Rolf; Blankenfeldt, Wulf
• Is Part Of: Acta crystallographica. Volume 72:Issue 8(2016:Aug.)
• Page Start: 652
• Page End: 658
• Publication Date: 2016-08-04
• Subjects: alternative isovaleryl coenzyme A biosynthesis -- medium‐chain dehydrogenase/reductase -- zinc‐dependence -- hexahistidine tag -- TEV protease‐recognition sequence -- Myxococcus xanthus; Crystallography -- Periodicals; Crystals -- Periodicals; 548
• DOI: 10.1107/S2053230X16011146
• Languages: English
• ISSNs: 2053-230X

Abstract

Abstract : The crystal structure of AibC, the terminal reductase in myxococcal de novo isovaleryl coenzyme A biosynthesis, has been determined at 2.55 Å resolution. Abstract : 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.