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TitleBacterial selenocysteine synthase structure revealed by single-particle cryoEM.
Journal, issue, pagesCurr Res Struct Biol, Vol. 7, Page 100143, Year 2024
Publish dateApr 16, 2024
AuthorsVitor Hugo Balasco Serrão / Karine Minari / Humberto D'Muniz Pereira / Otavio Henrique Thiemann /
PubMed AbstractThe 21st amino acid, selenocysteine (Sec), is synthesized on its dedicated transfer RNA (tRNA). In bacteria, Sec is synthesized from Ser-tRNA by Selenocysteine Synthase (SelA), which is a pivotal ...The 21st amino acid, selenocysteine (Sec), is synthesized on its dedicated transfer RNA (tRNA). In bacteria, Sec is synthesized from Ser-tRNA by Selenocysteine Synthase (SelA), which is a pivotal enzyme in the biosynthesis of Sec. The structural characterization of bacterial SelA is of paramount importance to decipher its catalytic mechanism and its role in the regulation of the Sec-synthesis pathway. Here, we present a comprehensive single-particle cryo-electron microscopy (SPA cryoEM) structure of the bacterial SelA with an overall resolution of 2.69 Å. Using recombinant SelA, we purified and prepared samples for single-particle cryoEM. The structural insights from SelA, combined with previous and knowledge, underscore the indispensable role of decamerization in SelA's function. Moreover, our structural analysis corroborates previous results that show that SelA adopts a pentamer of dimers configuration, and the active site architecture, substrate binding pocket, and key K295 catalytic residue are identified and described in detail. The differences in protein architecture and substrate coordination between the bacterial enzyme and its counterparts offer compelling structural evidence supporting the independent molecular evolution of the bacterial and archaea/eukarya Ser-Sec biosynthesis present in the natural world.
External linksCurr Res Struct Biol / PubMed:38681238 / PubMed Central
MethodsEM (single particle)
Resolution2.69 Å
Structure data

EMDB-42845, PDB-8uzw:
Selenocysteine synthase- SelA
Method: EM (single particle) / Resolution: 2.69 Å

Source
  • escherichia coli (E. coli)
KeywordsRNA BINDING PROTEIN / Selenocysteine / tRNASec / Sec-synthase

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