3gq1

<table><tr><td colspan='2'>[[3gq1]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Cauvi Cauvi]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3GQ1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3GQ1 FirstGlance]. <br>

</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>

<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3dnj|3dnj]], [[3g19|3g19]], [[3g1b|3g1b]], [[3gq0|3gq0]]</div></td></tr>

<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">CC_2467, clpS ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=155892 CAUVI])</td></tr>

[[https://www.uniprot.org/uniprot/CLPS_CAUCR CLPS_CAUCR]] Involved in the modulation of the specificity of the ClpAP-mediated ATP-dependent protein degradation (By similarity).

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== 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<ref>PMID:19451643</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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<div class="pdbe-citations 3gq1" style="background-color:#fffaf0;"></div>

== References ==

<references/>

[[Category: Cauvi]]

[[Category: Baker, T A]]

[[Category: Grant, R A]]

[[Category: Roman-Hernandez, G]]

[[Category: Sauer, R T]]

[[Category: Protein-peptide complex]]