4yjm: Difference between revisions
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==The apo | |||
<StructureSection load='4yjm' size='340' side='right' caption='[[4yjm]], [[Resolution|resolution]] 1.95Å' scene=''> | ==The apo structure of Agrobacterium tumefaciens ClpS2== | ||
<StructureSection load='4yjm' size='340' side='right'caption='[[4yjm]], [[Resolution|resolution]] 1.95Å' scene=''> | |||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4yjm]] is a 4 chain structure. 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 [ | <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=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.952Å</td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <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> | </table> | ||
== Function == | == 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®/PubMed®, 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__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Agrobacterium fabrum str. C58]] | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: | [[Category: Baker TA]] | ||
[[Category: | [[Category: Grant RA]] | ||
[[Category: | [[Category: Sauer RT]] | ||
[[Category: | [[Category: Stein B]] | ||
Latest revision as of 11:01, 27 September 2023
The apo structure of Agrobacterium tumefaciens ClpS2The apo structure of Agrobacterium tumefaciens ClpS2
Structural highlights
FunctionCLPS2_AGRFC Involved in the modulation of the specificity of the ClpAP-mediated ATP-dependent protein degradation. Publication Abstract from PubMedThe 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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