Journal:Acta Cryst F:S2053230X22007555
From Proteopedia
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EmGluRS shares ~97% sequence identity with EaGluRS but less than 39% sequence identity with any other structures in the Protein Data Bank. EmGluRS and EaGluRS have prototypical bacterial GluRS topology. EmGluRS and EaGluRS have similar binding sites and tertiary structures to other bacterial GluRS that are promising drug targets. These structural similarities can be exploited for drug discovery. | EmGluRS shares ~97% sequence identity with EaGluRS but less than 39% sequence identity with any other structures in the Protein Data Bank. EmGluRS and EaGluRS have prototypical bacterial GluRS topology. EmGluRS and EaGluRS have similar binding sites and tertiary structures to other bacterial GluRS that are promising drug targets. These structural similarities can be exploited for drug discovery. | ||
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| + | [[Image:Figures3q2.png|left|450px|thumb|Structural and primary sequence alignment of EaGluRS, EmGluRS, and PaGluRS. The secondary structure elements are as follows: α- helices are shown as large coils, 310 helices are shown in small coils labeled η, beta-strand are shown in arrows labeled β, and beta-turns are labeled TT. The identical residues are shown on a red background with conserved residues in red and conserved regions in blue boxes.]] | ||
| + | {{Clear}} | ||
<scene name='91/917942/Cv/8'>Superposed structures</scene> of PaGluRS (pdb entry [[5tgt]], yellow), EmGluRS (gray), and EaGluRS (cyan). | <scene name='91/917942/Cv/8'>Superposed structures</scene> of PaGluRS (pdb entry [[5tgt]], yellow), EmGluRS (gray), and EaGluRS (cyan). | ||
<jmol><jmolButton><script>frame 1 1 play; animation off; frame 1</script><text>only EmGluRS</text></jmolButton><jmolButton><script>frame 2 2 play; animation off; frame 2</script><text>only EaGluRS</text></jmolButton><jmolButton><script>frame 3 3 play; animation off; frame 3</script><text>only PaGluRS</text></jmolButton><jmolButton><script>animation off; frame all</script><text>EmGluRS, EaGluRS, and PaGluRS</text></jmolButton></jmol> | <jmol><jmolButton><script>frame 1 1 play; animation off; frame 1</script><text>only EmGluRS</text></jmolButton><jmolButton><script>frame 2 2 play; animation off; frame 2</script><text>only EaGluRS</text></jmolButton><jmolButton><script>frame 3 3 play; animation off; frame 3</script><text>only PaGluRS</text></jmolButton><jmolButton><script>animation off; frame all</script><text>EmGluRS, EaGluRS, and PaGluRS</text></jmolButton></jmol> | ||
| - | [[Image:Figures3q2.png|left|450px|thumb|Structural and primary sequence alignment of EaGluRS, EmGluRS, and PaGluRS. The secondary structure elements are as follows: α- helices are shown as large coils, 310 helices are shown in small coils labeled η, beta-strand are shown in arrows labeled β, and beta-turns are labeled TT. The identical residues are shown on a red background with conserved residues in red and conserved regions in blue boxes.]] | ||
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<b>References</b><br> | <b>References</b><br> | ||
<references/> | <references/> | ||
</StructureSection> | </StructureSection> | ||
__NOEDITSECTION__ | __NOEDITSECTION__ | ||
Revision as of 11:22, 28 July 2022
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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.
