Sandbox1313

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(New page: ==Lysyl-tRNA Synthase== Shown here is PDB number 1bbu, lysyl-tRNA Synthase shown here complexed with the lysine substrate. It consists of both "α-helices" and "β-strands" (the latter in ...)
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==Lysyl-tRNA Synthase==
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'''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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Shown here is PDB number 1bbu, lysyl-tRNA Synthase shown here complexed with the lysine substrate. It consists of both "α-helices" and "β-strands" (the latter in sheets and a barrel).
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As you can see in the "active site", the 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.
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{{STRUCTURE_1bbw| PDB=1bbw | SCENE=Sandbox1313/Defaultscene/1 }}==Lysyl-tRNA Synthase==
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It is also worth mentioning that when the lysine enters the complex, a small number of "residues" trigger a
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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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<applet load='1bbu' size='250' color='white' frame='true' align='left' caption='Lysine-bound lysyl-tRNA synthase' name='1bbu'/>
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{{STRUCTURE_1bbw | PDB=1bbw | SCENE= }}
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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,
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<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!


PDB ID 1bbw

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1bbw, resolution 2.70Å ()
Gene: LYSS (Escherichia coli)
Activity: Lysine--tRNA ligase, with EC number 6.1.1.6
Related: 1bbu
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.

Lysine-bound lysyl-tRNA synthase

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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.

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