4yjm: Difference between revisions

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-'''Unreleased structure'''
-The entry 4yjm is ON HOLD  until Paper Publication
+==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 [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=4YJM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4YJM 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]] 1.952&#8491;</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=4yjm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4yjm OCA], [https://pdbe.org/4yjm PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4yjm RCSB], [https://www.ebi.ac.uk/pdbsum/4yjm PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4yjm 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.
-Authors: Stein, B., Grant, R.A., Sauer, R.T., Baker, T.A.
+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>
-Description:
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-[[Category: Unreleased Structures]]
+</div>
-[[Category: Stein, B]]
+<div class="pdbe-citations 4yjm" style="background-color:#fffaf0;"></div>
-[[Category: Sauer, R.T]]
-[[Category: Baker, T.A]]
+==See Also==
-[[Category: Grant, R.A]]
+*[[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]]