Journal:Acta Cryst F:S2053230X19000815
From Proteopedia
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The GAD domain exists as an insertion in bacterial aminoacyl-tRNA synthetases (aaRSs), such as aspartyl- and glutamyl-tRNA synthetases (AspRS and GluRS). Structural comparison of Tdi1 with the GAD domain of E. coli AspRS (PDB ID [[1c0a]]) showed they have similar topology structures (with a RMSD of 3.9). <scene name='80/806371/Cv/12'>Structural superposition of Tdi1 with the GAD domain of E. coli AspRS</scene> (PDB ID [[1c0a]], in gray) shown as cartoon. An AMP molecule (shown as green sticks) is bound in ''E. coli'' AspRS. | The GAD domain exists as an insertion in bacterial aminoacyl-tRNA synthetases (aaRSs), such as aspartyl- and glutamyl-tRNA synthetases (AspRS and GluRS). Structural comparison of Tdi1 with the GAD domain of E. coli AspRS (PDB ID [[1c0a]]) showed they have similar topology structures (with a RMSD of 3.9). <scene name='80/806371/Cv/12'>Structural superposition of Tdi1 with the GAD domain of E. coli AspRS</scene> (PDB ID [[1c0a]], in gray) shown as cartoon. An AMP molecule (shown as green sticks) is bound in ''E. coli'' AspRS. | ||
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| + | <scene name='80/806371/Cv/13'>Structural superposition of Tdi1 (shown as the transparent spacefill charge) with the GAD domain of AspRS</scene> (only the AMP molecule is shown). An AMP molecule (shown in green spacefill representation) is bound in ''E. coli'' AspRS. The AMP is buried in Tdi1 and far from its positive groove, indicating Tdi1 may have a different active site from AspRS. | ||
<b>References</b><br> | <b>References</b><br> | ||
Revision as of 12:50, 21 January 2019
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This page complements a publication in scientific journals and is one of the Proteopedia's Interactive 3D Complement pages. For aditional details please see I3DC.
