|
|
| (One intermediate revision not shown.) |
| Line 3: |
Line 3: |
| | <StructureSection load='4yjm' size='340' side='right'caption='[[4yjm]], [[Resolution|resolution]] 1.95Å' scene=''> | | <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 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> | + | <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='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4yka|4yka]], [[4yjx|4yjx]]</td></tr> | + | </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='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'>[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> |
| - | <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> | | </table> |
| | == Function == | | == 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. | + | [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;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
| Line 26: |
Line 25: |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Agrfc]] | + | [[Category: Agrobacterium fabrum str. C58]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Baker, T A]] | + | [[Category: Baker TA]] |
| - | [[Category: Grant, R A]] | + | [[Category: Grant RA]] |
| - | [[Category: Sauer, R T]] | + | [[Category: Sauer RT]] |
| - | [[Category: Stein, B]] | + | [[Category: Stein B]] |
| - | [[Category: N-end rule]]
| + | |
| - | [[Category: Protease adaptor]]
| + | |
| - | [[Category: Protein binding]]
| + | |
| Structural highlights
Function
CLPS2_AGRFC Involved in the modulation of the specificity of the ClpAP-mediated ATP-dependent protein degradation.
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Stein BJ, Grant RA, Sauer RT, Baker TA. Structural Basis of an N-Degron Adaptor with More Stringent Specificity. Structure. 2016 Jan 20. pii: S0969-2126(15)00534-1. doi:, 10.1016/j.str.2015.12.008. PMID:26805523 doi:http://dx.doi.org/10.1016/j.str.2015.12.008
|
