Back to Search Start Over

Crystal structures of aconitase X enzymes from bacteria and archaea provide insights into the molecular evolution of the aconitase superfamily

Authors :
Kunihiko Tajima
Yasunori Watanabe
Yasuhiro Sakurai
Seiya Watanabe
Yohsuke Murase
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.

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