Crystal structure of AibC, a reductase involved in alternative de novo isovaleryl coenzyme A biosynthesis in Myxococcus xanthus.

2.50
Hdl Handle:
http://hdl.handle.net/10033/620559
Title:
Crystal structure of AibC, a reductase involved in alternative de novo isovaleryl coenzyme A biosynthesis in Myxococcus xanthus.
Authors:
Bock, Tobias; Müller, Rolf ( 0000-0002-1042-5665 ) ; Blankenfeldt, Wulf ( 0000-0001-9886-9668 )
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.
Affiliation:
Helmholtz Centre for infection research, Inhoffenstr. 7, 38124 Braunschweig, Germany.
Citation:
Crystal structure of AibC, a reductase involved in alternative de novo isovaleryl coenzyme A biosynthesis in Myxococcus xanthus. 2016, 72 (Pt 8):652-8 Acta Crystallogr F Struct Biol Commun
Journal:
Acta crystallographica. Section F, Structural biology communications
Issue Date:
Aug-2016
URI:
http://hdl.handle.net/10033/620559
DOI:
10.1107/S2053230X16011146
PubMed ID:
27487931
Type:
Article
ISSN:
2053-230X
Appears in Collections:
Publications of the Dept. Structure and Functions of Proteins(SFPR)

Full metadata record

DC FieldValue Language
dc.contributor.authorBock, Tobiasen
dc.contributor.authorMüller, Rolfen
dc.contributor.authorBlankenfeldt, Wulfen
dc.date.accessioned2016-10-20T09:42:10Z-
dc.date.available2016-10-20T09:42:10Z-
dc.date.issued2016-08-
dc.identifier.citationCrystal structure of AibC, a reductase involved in alternative de novo isovaleryl coenzyme A biosynthesis in Myxococcus xanthus. 2016, 72 (Pt 8):652-8 Acta Crystallogr F Struct Biol Communen
dc.identifier.issn2053-230X-
dc.identifier.pmid27487931-
dc.identifier.doi10.1107/S2053230X16011146-
dc.identifier.urihttp://hdl.handle.net/10033/620559-
dc.description.abstractIsovaleryl 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.en
dc.languageENG-
dc.rights.urihttp://creativecommons.org/licenses/by-nc-sa/4.0/*
dc.titleCrystal structure of AibC, a reductase involved in alternative de novo isovaleryl coenzyme A biosynthesis in Myxococcus xanthus.-
dc.typeArticleen
dc.contributor.departmentHelmholtz Centre for infection research, Inhoffenstr. 7, 38124 Braunschweig, Germany.en
dc.identifier.journalActa crystallographica. Section F, Structural biology communicationsen
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