Sandbox1313

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spinqualitylabelsall models Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D load='1bbw' size='350' frame='false' scene='Sandbox1313/Defaultscene/1'
1bbw, resolution 2.70Å (default scene)
Gene:	LYSS (Escherichia coli)
Activity:	Lysine--tRNA ligase, with EC number 6.1.1.6
Related:	1bbu
Structural annotation: Resources: CATH : 1Bbwa02, 1Bbwa01 InterPro : Ipr004364, Ipr006195, Ipr002313, Ipr012340, Ipr004365 Pfam : PF01336, PF00152 SCOP : d1bbwa2, d1bbwa1 UniProt : P0A8N3
Functional annotation: Cellular component: membrane fraction cytoplasm Biological process: tRNA aminoacylation for protein translation translation lysyl-tRNA aminoacylation Molecular function: nucleotide binding ATP binding metal ion binding aminoacyl-tRNA ligase activity magnesium ion binding ligase activity protein binding nucleic acid binding lysine-tRNA ligase activity
Evolutionary conservation: Toggle Conservation Colors: Rows = identical sequences: Further Information: Caveats, Explanation, Complete Results at ConSurfDB
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.

spinqualitylabelsall models Lysine-bound lysyl-tRNA synthase Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D

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.