3hl2 | pdb_00003hl2

The crystal structure of the human SepSecS-tRNASec complex

spinqualitylabelsall models 3hl2, resolution 2.81Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3hl2 is a 5 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: PLR, SEP, TS6 Gene: SEPSECS, TRNP48 (Homo sapiens) Activity: L-seryl-tRNA(Sec) selenium transferase, with EC number 2.9.1.1 Resources: FirstGlance, OCA, RCSB, PDBsum Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed Selenocysteine is the only genetically encoded amino acid in humans whose biosynthesis occurs on its cognate transfer RNA (tRNA). O-Phosphoseryl-tRNA:selenocysteinyl-tRNA synthase (SepSecS) catalyzes the final step of selenocysteine formation by a poorly understood tRNA-dependent mechanism. The crystal structure of human tRNA(Sec) in complex with SepSecS, phosphoserine, and thiophosphate, together with in vivo and in vitro enzyme assays, supports a pyridoxal phosphate-dependent mechanism of Sec-tRNA(Sec) formation. Two tRNA(Sec) molecules, with a fold distinct from other canonical tRNAs, bind to each SepSecS tetramer through their 13-base pair acceptor-TPsiC arm (where Psi indicates pseudouridine). The tRNA binding is likely to induce a conformational change in the enzyme's active site that allows a phosphoserine covalently attached to tRNA(Sec), but not free phosphoserine, to be oriented properly for the reaction to occur. The human SepSecS-tRNASec complex reveals the mechanism of selenocysteine formation.,Palioura S, Sherrer RL, Steitz TA, Soll D, Simonovic M Science. 2009 Jul 17;325(5938):321-5. PMID:19608919 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Selenocysteine Selenocysteine synthase

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