3GQ1
The structure of the caulobacter crescentus clpS protease adaptor protein in complex with a WLFVQRDSKE decapeptide
Summary for 3GQ1
| Entry DOI | 10.2210/pdb3gq1/pdb |
| Related | 3dnj 3G19 3G1B 3gq0 |
| Descriptor | ATP-dependent Clp protease adapter protein clpS, WLFVQRDSKE peptide, MAGNESIUM ION, ... (4 entities in total) |
| Functional Keywords | adaptor, protein-peptide complex, peptide-binding protein, peptide binding protein |
| Biological source | Caulobacter vibrioides (Caulobacter vibrioides) |
| Total number of polymer chains | 4 |
| Total formula weight | 22531.94 |
| Authors | Baker, T.A.,Roman-Hernandez, G.,Sauer, R.T.,Grant, R.A. (deposition date: 2009-03-23, release date: 2009-05-05, Last modification date: 2024-02-21) |
| Primary citation | Roman-Hernandez, G.,Grant, R.A.,Sauer, R.T.,Baker, T.A. Molecular basis of substrate selection by the N-end rule adaptor protein ClpS. Proc.Natl.Acad.Sci.USA, 106:8888-8893, 2009 Cited by PubMed Abstract: 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. PubMed: 19451643DOI: 10.1073/pnas.0903614106 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.496 Å) |
Structure validation
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