Sandbox1313: Difference between revisions
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{{STRUCTURE_1bbw | PDB=1bbw | SCENE= }} | {{STRUCTURE_1bbw | PDB=1bbw | SCENE= }} | ||
{{STRUCTURE_1bbw| PDB=1bbw | SCENE= }} | |||
==Lysyl-tRNA Synthase== | ==Lysyl-tRNA Synthase== | ||
Shown here is PDB number 1bbu, lysyl-tRNA Synthase shown here complexed with the lysine substrate. It consists of both <scene name='Sandbox1313/Alpha_and_beta_strands/1'>alpha helices and beta sheets</scene> (the latter in sheets and a barrel). Below is pictured the exact same synthase complexed with it's residue of interest, lysine. | Shown here is PDB number 1bbu, lysyl-tRNA Synthase shown here complexed with the lysine substrate. It consists of both <scene name='Sandbox1313/Alpha_and_beta_strands/1'>alpha helices and beta sheets</scene> (the latter in sheets and a barrel). Below is pictured the exact same synthase complexed with it's residue of interest, lysine. | ||
<applet load='1bbu' size=' | <applet load='1bbu' size='250' color='white' frame='true' align='left' caption='Lysine-bound lysyl-tRNA synthase' name='1bbu'/> | ||
<scene name='Sandbox1313/Hydrogen_bonding_partners/1'>these residues</scene> trigger a complex conformational change that completely changes the synthase. These changes involve | In the active site, the bound lysine participates in multiple hydrogen bonding interactions to stay complexed to the synthase protein as it moves into position to build the tRNA in the ribosome. Specifically, | ||
<scene name='Sandbox1313/Hydrogen_bonding_partners/1'>these residues</scene> trigger a complex conformational change that completely changes the shape of part of the synthase. These changes involve <scene name='Sandbox1313/These_two_loops/1'>these two loops</scene> and some <scene name='Sandbox1313/Other_pieces/1'>other pieces</scene> of the molecule. This conformational change effectively closes the active site when bound to lysine. | |||
Revision as of 22:46, 12 May 2009
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| 1bbw, resolution 2.70Å (default scene) | |||||||||||||
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| Gene: | LYSS (Escherichia coli) | ||||||||||||
| Activity: | Lysine--tRNA ligase, with EC number 6.1.1.6 | ||||||||||||
| Related: | 1bbu | ||||||||||||
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||||||
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| 1bbw, resolution 2.70Å (default scene) | |||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Gene: | LYSS (Escherichia coli) | ||||||||||||
| Activity: | Lysine--tRNA ligase, with EC number 6.1.1.6 | ||||||||||||
| Related: | 1bbu | ||||||||||||
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||||||
Lysyl-tRNA Synthase
Shown here is PDB number 1bbu, lysyl-tRNA Synthase shown here complexed with the lysine substrate. It consists of both alpha helices and beta sheets (the latter in sheets and a barrel). Below is pictured the exact same synthase complexed with it's residue of interest, lysine.
|
In the active site, the bound lysine participates in multiple hydrogen bonding interactions to stay complexed to the synthase protein as it moves into position to build the tRNA in the ribosome. Specifically, these residues trigger a complex conformational change that completely changes the shape of part of the synthase. These changes involve these two loops and some other pieces of the molecule. This conformational change effectively closes the active site when bound to lysine.
