Traces of convergent evolution left in the structure of EgtB-IV

Taku Mizutani; Ikuro Abe

doi:10.1016/j.str.2024.10.006

Traces of convergent evolution left in the structure of EgtB-IV

Structure. 2024 Nov 7;32(11):1854-1856. doi: 10.1016/j.str.2024.10.006.

Authors

Taku Mizutani¹, Ikuro Abe²

Affiliations

¹ Graduate School of Pharmaceutical Sciences, The University of Tokyo, 7-3-1 Hongo, Bunkyo-ku, Tokyo 113-0033, Japan.
² Graduate School of Pharmaceutical Sciences, The University of Tokyo, 7-3-1 Hongo, Bunkyo-ku, Tokyo 113-0033, Japan; Collaborative Research Institute for Innovative Microbiology, The University of Tokyo, Yayoi 1-1-1, Bunkyo-ku, Tokyo 113-8657, Japan. Electronic address: [email protected].

PMID: 39515304
DOI: 10.1016/j.str.2024.10.006

Abstract

The enzymatically regioselective catalyzed incorporation of cysteine sulfoxide into histidine generates physiologically important antioxidants such as ergothioneine and ovothiol. In this issue of Structure, Ireland et al.¹ report the crystal structure of EgtB-IV, which provides insights into the convergent evolution of sulfoxide synthase.

MeSH terms

Bacterial Proteins / chemistry
Bacterial Proteins / genetics
Bacterial Proteins / metabolism
Crystallography, X-Ray
Cysteine / chemistry
Cysteine / metabolism
Evolution, Molecular*
Histidine / chemistry
Histidine / metabolism
Models, Molecular

Substances

Bacterial Proteins
Cysteine
Histidine