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Crystal structures of aconitase X enzymes from bacteria and archaea provide insights into the molecular evolution of the aconitase superfamily
- Source :
- Communications Biology, Vol 4, Iss 1, Pp 1-15 (2021), Communications Biology
- Publication Year :
- 2021
- Publisher :
- Springer Science and Business Media LLC, 2021.
-
Abstract
- Aconitase superfamily members catalyze the homologous isomerization of specific substrates by sequential dehydration and hydration and contain a [4Fe-4S] cluster. However, monomeric and heterodimeric types of function unknown aconitase X (AcnX) have recently been characterized as a cis-3-hydroxy-L-proline dehydratase (AcnXType-I) and mevalonate 5-phosphate dehydratase (AcnXType-II), respectively. We herein elucidated the crystal structures of AcnXType-I from Agrobacterium tumefaciens (AtAcnX) and AcnXType-II from Thermococcus kodakarensis (TkAcnX) without a ligand and in complex with substrates. AtAcnX and TkAcnX contained the [2Fe-2S] and [3Fe-4S] clusters, respectively, conforming to UV and EPR spectroscopy analyses. The binding sites of the [Fe-S] cluster and substrate were clearlydifferent from those that were completely conserved in other aconitase enzymes; however, theoverall structural frameworks and locations of active sites were partially similar to each other.These results provide novel insights into the evolutionary scenario of the aconitase superfamilybased on the recruitment hypothesis.<br />Seiya Watanabe et al. report the crystal structures of two distinct members of the Aconitase X subfamily, which contain [Fe-S] clusters different from other aconitases. This study provides insight into the molecular evolution of the aconitase superfamily.
- Subjects :
- Models, Molecular
0301 basic medicine
Subfamily
Protein Conformation
QH301-705.5
Stereochemistry
Medicine (miscellaneous)
Crystallography, X-Ray
Aconitase
Article
General Biochemistry, Genetics and Molecular Biology
Evolution, Molecular
03 medical and health sciences
0302 clinical medicine
Molecular evolution
Catalytic Domain
Biology (General)
Binding site
X-ray crystallography
Aconitate Hydratase
chemistry.chemical_classification
biology
Chemistry
biology.organism_classification
Ligand (biochemistry)
Enzymes
Thermococcus kodakarensis
Thermococcus
030104 developmental biology
Enzyme
Agrobacterium tumefaciens
Dehydratase
Enzyme mechanisms
General Agricultural and Biological Sciences
030217 neurology & neurosurgery
Subjects
Details
- ISSN :
- 23993642
- Volume :
- 4
- Database :
- OpenAIRE
- Journal :
- Communications Biology
- Accession number :
- edsair.doi.dedup.....4c172d56648299c936983e3edea1eb0f
- Full Text :
- https://doi.org/10.1038/s42003-021-02147-5