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3dnj

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==The structure of the Caulobacter crescentus ClpS protease adaptor protein in complex with a N-end rule peptide==
==The structure of the Caulobacter crescentus ClpS protease adaptor protein in complex with a N-end rule peptide==
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<StructureSection load='3dnj' size='340' side='right' caption='[[3dnj]], [[Resolution|resolution]] 1.15&Aring;' scene=''>
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<StructureSection load='3dnj' size='340' side='right'caption='[[3dnj]], [[Resolution|resolution]] 1.15&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[3dnj]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Cauce Cauce]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3DNJ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3DNJ FirstGlance]. <br>
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<table><tr><td colspan='2'>[[3dnj]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Caulobacter_vibrioides Caulobacter vibrioides]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3DNJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3DNJ FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.15&#8491;</td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">clpS, CC_2467 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=155892 CAUCE])</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
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<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=3dnj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3dnj OCA], [http://pdbe.org/3dnj PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3dnj RCSB], [http://www.ebi.ac.uk/pdbsum/3dnj PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3dnj ProSAT]</span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3dnj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3dnj OCA], [https://pdbe.org/3dnj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3dnj RCSB], [https://www.ebi.ac.uk/pdbsum/3dnj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3dnj ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/CLPS_CAUCR CLPS_CAUCR]] Involved in the modulation of the specificity of the ClpAP-mediated ATP-dependent protein degradation (By similarity).
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[https://www.uniprot.org/uniprot/CLPS_CAUVC CLPS_CAUVC] Involved in the modulation of the specificity of the ClpAP-mediated ATP-dependent protein degradation.[HAMAP-Rule:MF_00302]
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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The N-end rule targets specific proteins for destruction in prokaryotes and eukaryotes. Here, we report a crystal structure of a bacterial N-end rule adaptor, ClpS, bound to a peptide mimic of an N-end rule substrate. This structure, which was solved at a resolution of 1.15 A, reveals specific recognition of the peptide alpha-amino group via hydrogen bonding and shows that the peptide's N-terminal tyrosine side chain is buried in a deep hydrophobic cleft that pre-exists on the surface of ClpS. The adaptor side chains that contact the peptide's N-terminal residue are highly conserved in orthologs and in E3 ubiquitin ligases that mediate eukaryotic N-end rule recognition. We show that mutation of critical ClpS contact residues abrogates substrate delivery to and degradation by the AAA+ protease ClpAP, demonstrate that modification of the hydrophobic pocket results in altered N-end rule specificity, and discuss functional implications for the mechanism of substrate delivery.
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The molecular basis of N-end rule recognition.,Wang KH, Roman-Hernandez G, Grant RA, Sauer RT, Baker TA Mol Cell. 2008 Nov 7;32(3):406-14. PMID:18995838<ref>PMID:18995838</ref>
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==See Also==
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*[[ATP-dependent Clp protease adaptor protein 3D structures|ATP-dependent Clp protease adaptor protein 3D structures]]
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 3dnj" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Cauce]]
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[[Category: Caulobacter vibrioides]]
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[[Category: Baker, T A]]
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[[Category: Large Structures]]
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[[Category: Grant, R A]]
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[[Category: Baker TA]]
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[[Category: Roman-Hernandez, G]]
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[[Category: Grant RA]]
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[[Category: Sauer, R T]]
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[[Category: Roman-Hernandez G]]
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[[Category: Wang, K]]
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[[Category: Sauer RT]]
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[[Category: Adaptor]]
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[[Category: Wang K]]
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[[Category: Peptide binding protein]]
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[[Category: Protein-peptide complex]]
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Current revision

The structure of the Caulobacter crescentus ClpS protease adaptor protein in complex with a N-end rule peptide

PDB ID 3dnj

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