Journal:Acta Cryst F:S2053230X19000815
From Proteopedia
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The molecular surface representation of Tdi1 (blue, positive; red, negative), <scene name='80/806371/Cv/6'>colored by its local electrostatic potential</scene>. Remarkably, there is a groove that is mainly composed of β7, η1 and α5 in the GAD-like domain and extends to β8 in theDUF1851 domain. Many of the residues constituting the groove are conserved or highly conserved among Tdi1 homologs. Inspection of the surface charge distribution of the groove revealed it is covered with dominantly positive charges, which may be associated with nucleotide-binding. | The molecular surface representation of Tdi1 (blue, positive; red, negative), <scene name='80/806371/Cv/6'>colored by its local electrostatic potential</scene>. Remarkably, there is a groove that is mainly composed of β7, η1 and α5 in the GAD-like domain and extends to β8 in theDUF1851 domain. Many of the residues constituting the groove are conserved or highly conserved among Tdi1 homologs. Inspection of the surface charge distribution of the groove revealed it is covered with dominantly positive charges, which may be associated with nucleotide-binding. | ||
| - | <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. |
<b>References</b><br> | <b>References</b><br> | ||
Revision as of 12:30, 20 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.
