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    Brookhaven Instruments e coli asprs yeast trnaasp aspartyl adenylate
    Fig. 5. ( A ) Stereoview of the active site area of E.coli <t>AspRS</t> with bound yeast tRNA Asp and <t>aspartyl-adenylate.</t> The (2 F o – F c ) electron density map contoured at 1σ shows the aspartyl-adenylate substrate sitting on the antiparallel β-sheet of the catalytic domain. The flipping loop (residues 167–174 colored in blue) adopts a closed conformation. The contribution of this loop is essential to the binding of the aspartyl-adenylate and tRNA terminal adenosine substrates. (B–D) Conformation of the flipping loop and the tRNA terminal adenosine in ( B ) the yeast AspRS–yeast tRNA Asp complex, ( C ) the heterologous E.coli AspRS–yeast tRNA Asp complex and ( D ) the E.coli AspRS– E.coli tRNA Asp complex. The aspartyl-adenylate substrate is present in all three complexes.
    E Coli Asprs Yeast Trnaasp Aspartyl Adenylate, supplied by Brookhaven Instruments, used in various techniques. Bioz Stars score: 85/100, based on 2 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/e coli asprs yeast trnaasp aspartyl adenylate/product/Brookhaven Instruments
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    e coli asprs yeast trnaasp aspartyl adenylate - by Bioz Stars, 2020-11
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    Fig. 5. ( A ) Stereoview of the active site area of E.coli AspRS with bound yeast tRNA Asp and aspartyl-adenylate. The (2 F o – F c ) electron density map contoured at 1σ shows the aspartyl-adenylate substrate sitting on the antiparallel β-sheet of the catalytic domain. The flipping loop (residues 167–174 colored in blue) adopts a closed conformation. The contribution of this loop is essential to the binding of the aspartyl-adenylate and tRNA terminal adenosine substrates. (B–D) Conformation of the flipping loop and the tRNA terminal adenosine in ( B ) the yeast AspRS–yeast tRNA Asp complex, ( C ) the heterologous E.coli AspRS–yeast tRNA Asp complex and ( D ) the E.coli AspRS– E.coli tRNA Asp complex. The aspartyl-adenylate substrate is present in all three complexes.

    Journal: The EMBO Journal

    Article Title: The structure of an AspRS-tRNAAsp complex reveals a tRNA-dependent control mechanism

    doi: 10.1093/emboj/20.18.5290

    Figure Lengend Snippet: Fig. 5. ( A ) Stereoview of the active site area of E.coli AspRS with bound yeast tRNA Asp and aspartyl-adenylate. The (2 F o – F c ) electron density map contoured at 1σ shows the aspartyl-adenylate substrate sitting on the antiparallel β-sheet of the catalytic domain. The flipping loop (residues 167–174 colored in blue) adopts a closed conformation. The contribution of this loop is essential to the binding of the aspartyl-adenylate and tRNA terminal adenosine substrates. (B–D) Conformation of the flipping loop and the tRNA terminal adenosine in ( B ) the yeast AspRS–yeast tRNA Asp complex, ( C ) the heterologous E.coli AspRS–yeast tRNA Asp complex and ( D ) the E.coli AspRS– E.coli tRNA Asp complex. The aspartyl-adenylate substrate is present in all three complexes.

    Article Snippet: Coordinates for the X-ray structure of the E.coli AspRS–yeast tRNAAsp –aspartyl-adenylate have been deposited in the Brookhaven Protein Data Bank under accession code 1IL2.

    Techniques: Binding Assay