title: Se-ing into selenocysteine biosynthesis.
abstract: A cocrystal structure of the enzyme that synthesizes selenocysteine reveals the elegantly simple recognition mechanism for the tRNA molecule for this '21st amino acid'. The structure resolves some mechanistic questions and allows for comparison of the tRNA-dependent synthesis of cysteine and selenocysteine.
authors.affiliation: Department of Chemistry, University of Louisville, Louisville, Kentucky, USA. eugene.mueller@louisville.edu
authors.forename: Eugene G
authors.initials: EG
authors.lastname: Mueller
mesh_terms: D000604:Amino Acyl-tRNA Synthetases / Q000378:metabolism; D000818:Animals; D001426:Bacterial Proteins / Q000096:biosynthesis / Q000737:chemistry / Q000235:genetics; D003461:Crystallography; D006801:Humans; D006860:Hydrogen Bonding; D008958:Models, Molecular; D011487:Protein Conformation; D012345:RNA, Transfer, Amino Acid-Specific / Q000378:metabolism*; D017279:Selenocysteine / Q000096:biosynthesis* / Q000737:chemistry / Q000235:genetics; D013379:Substrate Specificity
chemical_list: D001426:Bacterial Proteins; D012345:RNA, Transfer, Amino Acid-Specific; C036928:tRNA, selenocysteine-; D017279:Selenocysteine; D000604:Amino Acyl-tRNA Synthetases; C542370:O-phosphoseryl-tRNA:selenocysteinyl-tRNA synthase, human
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