View source for 4yjm


==The apo structure of Agrobacterium tumefaciens ClpS2==
<StructureSection load='4yjm' size='340' side='right'caption='[[4yjm]], [[Resolution|resolution]] 1.95&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4yjm]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Agrfc Agrfc]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4YJM OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4YJM FirstGlance]. <br>
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4yka|4yka]], [[4yjx|4yjx]]</td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">clpS2, Atu2232, AGR_C_4060 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=176299 AGRFC])</td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4yjm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4yjm OCA], [http://pdbe.org/4yjm PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4yjm RCSB], [http://www.ebi.ac.uk/pdbsum/4yjm PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4yjm ProSAT]</span></td></tr>
</table>
== Function ==
[[http://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 4yjm" 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: Agrfc]]
[[Category: Large Structures]]
[[Category: Baker, T A]]
[[Category: Grant, R A]]
[[Category: Sauer, R T]]
[[Category: Stein, B]]
[[Category: N-end rule]]
[[Category: Protease adaptor]]
[[Category: Protein binding]]