View source for 4yjx


==The structure of Agrobacterium tumefaciens ClpS2 bound to L-phenylalaninamide==
<StructureSection load='4yjx' size='340' side='right'caption='[[4yjx]], [[Resolution|resolution]] 2.55&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4yjx]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Agrobacterium_fabrum_str._C58 Agrobacterium fabrum str. C58]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4YJX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4YJX FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.547&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NFA:PHENYLALANINE+AMIDE'>NFA</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4yjx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4yjx OCA], [https://pdbe.org/4yjx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4yjx RCSB], [https://www.ebi.ac.uk/pdbsum/4yjx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4yjx ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/CLPS2_AGRFC CLPS2_AGRFC] Involved in the modulation of the specificity of the ClpAP-mediated ATP-dependent protein degradation.
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The N-end rule dictates that a protein's N-terminal residue determines its half-life. In bacteria, the ClpS adaptor mediates N-end-rule degradation, by recognizing proteins bearing specific N-terminal residues and delivering them to the ClpAP AAA+ protease. Unlike most bacterial clades, many alpha-proteobacteria encode two ClpS paralogs, ClpS1 and ClpS2. Here, we demonstrate that both ClpS1 and ClpS2 from A. tumefaciens deliver N-end-rule substrates to ClpA, but ClpS2 has more stringent binding specificity, recognizing only a subset of the canonical bacterial N-end-rule residues. The basis of this enhanced specificity is addressed by crystal structures of ClpS2, with and without ligand, and structure-guided mutagenesis, revealing protein conformational changes and remodeling in the substrate-binding pocket. We find that ClpS1 and ClpS2 are differentially expressed during growth in A. tumefaciens and conclude that the use of multiple ClpS paralogs allows fine-tuning of N-end-rule degradation at the level of substrate recognition.

Structural Basis of an N-Degron Adaptor with More Stringent Specificity.,Stein BJ, Grant RA, Sauer RT, Baker TA Structure. 2016 Jan 20. pii: S0969-2126(15)00534-1. doi:, 10.1016/j.str.2015.12.008. PMID:26805523<ref>PMID:26805523</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4yjx" style="background-color:#fffaf0;"></div>

==See Also==
*[[ATP-dependent Clp protease adaptor protein 3D structures|ATP-dependent Clp protease adaptor protein 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Agrobacterium fabrum str. C58]]
[[Category: Large Structures]]
[[Category: Baker TA]]
[[Category: Grant RA]]
[[Category: Sauer RT]]
[[Category: Stein B]]