2w9r

STRUCTURAL BASIS OF N-END RULE SUBSTRATE RECOGNITION IN ESCHERICHIA COLI BY THE CLPAP ADAPTOR PROTEIN CLPS

spinqualitylabelsall models 2w9r, resolution 1.70Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2w9r is a 2 chain structure with sequence from Escherichia coli. Full crystallographic information is available from OCA. Related: 1lzw, 1mbu, 1jre, 1l8h, 1mg9, 1mbv, 1l8i, 1r6o, 1jts, 1f33, 1f30, 1r6q, 1mbx, 1dps Activity: Glucokinase, with EC number 2.7.1.2 Resources: FirstGlance, OCA, RCSB, PDBsum Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed In Escherichia coli, the ClpAP protease, together with the adaptor protein ClpS, is responsible for the degradation of proteins bearing an amino-terminal destabilizing amino acid (N-degron). Here, we determined the three-dimensional structures of ClpS in complex with three peptides, each having a different destabilizing residue--Leu, Phe or Trp--at its N terminus. All peptides, regardless of the identity of their N-terminal residue, are bound in a surface pocket on ClpS in a stereo-specific manner. Several highly conserved residues in this binding pocket interact directly with the backbone of the N-degron peptide and hence are crucial for the binding of all N-degrons. By contrast, two hydrophobic residues define the volume of the binding pocket and influence the specificity of ClpS. Taken together, our data suggest that ClpS has been optimized for the binding and delivery of N-degrons containing an N-terminal Phe or Leu. Structural basis of N-end rule substrate recognition in Escherichia coli by the ClpAP adaptor protein ClpS.,Schuenemann VJ, Kralik SM, Albrecht R, Spall SK, Truscott KN, Dougan DA, Zeth K EMBO Rep. 2009 May;10(5):508-14. Epub 2009 Apr 17. PMID:19373253 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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