Sandbox1313

From Proteopedia

This sandbox is in use until June 1, 2009 for UMass Chemistry 490a. Others please do not edit this page. Thanks!

spinqualitylabelsall models PDB ID 1bbw Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image
1bbw, resolution 2.70Å ()
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 (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, 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.