3gq1 | pdb_00003gq1

The structure of the caulobacter crescentus clpS protease adaptor protein in complex with a WLFVQRDSKE decapeptide

spinqualitylabelsall models 3gq1, resolution 1.50Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3gq1 is a 4 chain structure with sequence from Cauvi. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: MG Related: 3dnj, 3g19, 3g1b, 3gq0 Gene: CC_2467, clpS (CAUVI) Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [CLPS_CAUCR] Involved in the modulation of the specificity of the ClpAP-mediated ATP-dependent protein degradation (By similarity). 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 The N-end rule is a conserved degradation pathway that relates the stability of a protein to its N-terminal amino acid. Here, we present crystal structures of ClpS, the bacterial N-end rule adaptor, alone and engaged with peptides containing N-terminal phenylalanine, leucine, and tryptophan. These structures, together with a previous structure of ClpS bound to an N-terminal tyrosine, illustrate the molecular basis of recognition of the complete set of primary N-end rule amino acids. In each case, the alpha-amino group and side chain of the N-terminal residue are the major determinants of recognition. The binding pocket for the N-end residue is preformed in the free adaptor, and only small adjustments are needed to accommodate N-end rule residues having substantially different sizes and shapes. M53A ClpS is known to mediate degradation of an expanded repertoire of substrates, including those with N-terminal valine or isoleucine. A structure of Met53A ClpS engaged with an N-end rule tryptophan reveals an essentially wild-type mechanism of recognition, indicating that the Met(53) side chain directly enforces specificity by clashing with and excluding beta-branched side chains. Finally, experimental and structural data suggest mechanisms that make proteins with N-terminal methionine bind very poorly to ClpS, explaining why these high-abundance proteins are not degraded via the N-end rule pathway in the cell. Molecular basis of substrate selection by the N-end rule adaptor protein ClpS.,Roman-Hernandez G, Grant RA, Sauer RT, Baker TA Proc Natl Acad Sci U S A. 2009 Jun 2;106(22):8888-93. Epub 2009 May 18. PMID:19451643 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also ATP-dependent Clp protease adaptor protein 3D structures

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