Journal:Acta Cryst F:S2053230X22007555
From Proteopedia
(Difference between revisions)
| (21 intermediate revisions not shown.) | |||
| Line 1: | Line 1: | ||
| - | <StructureSection load='' size='450' side='right' scene='91/917942/ | + | <StructureSection load='' size='450' side='right' scene='91/917942/Cv2/1' caption=''> |
===Crystal structures of glutamyl-tRNA synthetase from ''Elizabethkingia anopheles'' and ''E. meningosepticum''=== | ===Crystal structures of glutamyl-tRNA synthetase from ''Elizabethkingia anopheles'' and ''E. meningosepticum''=== | ||
<big>Lauryn Brooks, Sandhya Subramanian, David M. Dranow, Stephen J. Mayclin, Peter J. Myler, and Oluwatoyin A. Asojo</big> <ref>doi: 10.1107/S2053230X22007555</ref> | <big>Lauryn Brooks, Sandhya Subramanian, David M. Dranow, Stephen J. Mayclin, Peter J. Myler, and Oluwatoyin A. Asojo</big> <ref>doi: 10.1107/S2053230X22007555</ref> | ||
<hr/> | <hr/> | ||
<b>Molecular Tour</b><br> | <b>Molecular Tour</b><br> | ||
| - | ''Elizabethkingia'' bacteria are emerging pathogens globally that cause opportunistic and nosocomial infections with up to 40% mortality among the immune-compromised. ''Elizabethkingia'' species are in the pipeline of organisms for high throughput structural analysis at the Seattle Structural Genomics Center for Infectious Disease (SSGCID). These efforts include the structure-function analysis of potential therapeutic targets. Glutamyl-tRNA synthetase (GluRS) is essential to the tRNA aminoacylation and is investigated as a bacterial drug target. The SSGCID produced crystallized and determined high-resolution structures of GluRS from ''Elizabethkingia meningosepticum'' (EmGluRS) and ''Elizabethkingia anopheles'' (EaGluRS). EmGluRS was co-crystallized with glutamate, while EaGluRS is an apo-structure. | + | ''Elizabethkingia'' bacteria are emerging pathogens globally that cause opportunistic and nosocomial infections with up to 40% mortality among the immune-compromised. ''Elizabethkingia'' species are in the pipeline of organisms for high throughput structural analysis at the Seattle Structural Genomics Center for Infectious Disease (SSGCID). These efforts include the structure-function analysis of potential therapeutic targets. Glutamyl-tRNA synthetase (GluRS) is essential to the tRNA aminoacylation and is investigated as a bacterial drug target. The SSGCID produced crystallized and determined high-resolution structures of GluRS from ''Elizabethkingia meningosepticum'' (EmGluRS; [[6brl]]) and ''Elizabethkingia anopheles'' (EaGluRS; [[6b1z]]). EmGluRS was co-crystallized with glutamate, while EaGluRS is an apo-structure. |
<scene name='91/917942/Cv/3'>EmGluRS monomer</scene> has a HUP-domain (orange), a Zn-binding-domain (green), and an anticodon binding domain (blue). The HUP domain and Zn-binding domain make up the N-terminal tRNA synthetases binding domain that binds the glutamate (spheres). | <scene name='91/917942/Cv/3'>EmGluRS monomer</scene> has a HUP-domain (orange), a Zn-binding-domain (green), and an anticodon binding domain (blue). The HUP domain and Zn-binding domain make up the N-terminal tRNA synthetases binding domain that binds the glutamate (spheres). | ||
| Line 13: | Line 13: | ||
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. | ||
| - | <scene name='91/917942/Cv/ | + | [[Image:Figures3q2.png|left|400px|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.]] |
| - | <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 | + | {{Clear}} |
| + | [[Image:Figqqqq.png|left|200px|thumb|Ribbon diagram calculated by ENDScript. Circumference of the ribbon (sausage) represents relative structural conservation compared to other GluRS structures. Thinner ribbons represent higher conserved regions, while thicker ribbons represent lower conserved regions.]] | ||
| + | {{Clear}} | ||
| + | <scene name='91/917942/Cv/17'>Spacefill representation of EmGluRS</scene> colored by sequence conservation with red indicating identical residues. Atoms of glutamate are colored in CPK. | ||
| + | |||
| + | <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> | ||
<b>References</b><br> | <b>References</b><br> | ||
Current revision
| |||||||||||
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.
