Sandbox1313
From Proteopedia
(→Lysyl-tRNA Synthase) |
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| - | {{STRUCTURE_1bbw | | + | '''This sandbox is in use until June 1, 2009 for UMass Chemistry 490a. Others please do not edit this page. Thanks!''' |
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| + | {{STRUCTURE_1bbw| PDB=1bbw | SCENE=Sandbox1313/Defaultscene/1 }}==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. | ||
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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, | 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/ | + | <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/2'>other pieces</scene> of the molecule. This conformational change effectively closes the active site when bound to lysine. |
Current revision
This sandbox is in use until June 1, 2009 for UMass Chemistry 490a. Others please do not edit this page. Thanks!
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| 1bbw, resolution 2.70Å () | |||||||||
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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 | ||||||||
Lysyl-tRNA Synthase
Shown here is PDB number 1bbu, lysyl-tRNA Synthase shown here complexed with the lysine substrate. It consists of both (the latter in sheets and a barrel). Below is pictured the exact same synthase complexed with it's residue of interest, lysine.
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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, trigger a complex conformational change that completely changes the shape of part of the synthase. These changes involve and some of the molecule. This conformational change effectively closes the active site when bound to lysine.
