Dimer–Dimer Interaction of the Bacterial Selenocysteine Synthase SelA Promotes Functional Active-Site Formation and Catalytic Specificity

The 21st amino acid, selenocysteine (Sec), is incorporated translationally into proteins and is synthesized on its specific tRNA (tRNASec). In Bacteria, the selenocysteine synthase SelA converts Ser-tRNASec, formed by seryl-tRNA synthetase, to Sec-tRNASec. SelA, a member of the fold-type-I pyridoxal...

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Veröffentlicht in:	Journal of molecular biology 2014-04, Vol.426 (8), p.1723-1735
Hauptverfasser:	Itoh, Yuzuru, Bröcker, Markus J., Sekine, Shun-ichi, Söll, Dieter, Yokoyama, Shigeyuki
Format:	Artikel
Sprache:	eng
Schlagworte:	21st amino acid Aquifex aeolicus Bacteria Bacterial Proteins - chemistry Bacterial Proteins - genetics Bacterial Proteins - metabolism Catalytic Domain - genetics Crystallography, X-Ray Escherichia coli - genetics Escherichia coli - metabolism Escherichia coli Proteins - chemistry Escherichia coli Proteins - genetics Escherichia coli Proteins - metabolism Evolution, Molecular fold-type-I PLP-dependent enzyme Models, Molecular Mutagenesis, Site-Directed pentamer of dimers Phylogeny Protein Interaction Domains and Motifs Protein Structure, Quaternary RNA, Transfer, Amino Acyl - chemistry RNA, Transfer, Amino Acyl - metabolism selenium metabolism Transferases - chemistry Transferases - genetics Transferases - metabolism tRNASec
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