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3o1f

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==P1 crystal form of E. coli ClpS at 1.4 A resolution==
==P1 crystal form of E. coli ClpS at 1.4 A resolution==
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<StructureSection load='3o1f' size='340' side='right' caption='[[3o1f]], [[Resolution|resolution]] 1.40&Aring;' scene=''>
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<StructureSection load='3o1f' size='340' side='right'caption='[[3o1f]], [[Resolution|resolution]] 1.40&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[3o1f]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3O1F OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3O1F FirstGlance]. <br>
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<table><tr><td colspan='2'>[[3o1f]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3O1F OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3O1F FirstGlance]. <br>
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</td></tr><tr><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=SME:METHIONINE+SULFOXIDE'>SME</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]] 1.4&#8491;</td></tr>
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<tr><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">clpS ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli])</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=SME:METHIONINE+SULFOXIDE'>SME</scene></td></tr>
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<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3o1f FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3o1f OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3o1f RCSB], [http://www.ebi.ac.uk/pdbsum/3o1f PDBsum]</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=3o1f FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3o1f OCA], [https://pdbe.org/3o1f PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3o1f RCSB], [https://www.ebi.ac.uk/pdbsum/3o1f PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3o1f ProSAT]</span></td></tr>
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<table>
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</table>
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<div style="background-color:#fffaf0;">
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== Function ==
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== Publication Abstract from PubMed ==
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[https://www.uniprot.org/uniprot/CLPS_ECOLI CLPS_ECOLI] Involved in the modulation of the specificity of the ClpAP-mediated ATP-dependent protein degradation.
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The ClpS adaptor delivers N-end rule substrates to ClpAP, an energy-dependent AAA+ protease, for degradation. How ClpS binds specific N-end residues is known in atomic detail and clarified here, but the delivery mechanism is poorly understood. We show that substrate binding is enhanced when ClpS binds hexameric ClpA. Reciprocally, N-end rule substrates increase ClpS affinity for ClpA(6). Enhanced binding requires the N-end residue and a peptide bond of the substrate, as well as multiple aspects of ClpS, including a side chain that contacts the substrate alpha-amino group and the flexible N-terminal extension (NTE). Finally, enhancement also needs the N domain and AAA+ rings of ClpA, connected by a long linker. The NTE can be engaged by the ClpA translocation pore, but ClpS resists unfolding/degradation. We propose a staged-delivery model that illustrates how intimate contacts between the substrate, adaptor, and protease reprogram specificity and coordinate handoff from the adaptor to the protease.
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The ClpS Adaptor Mediates Staged Delivery of N-End Rule Substrates to the AAA+ ClpAP Protease.,Roman-Hernandez G, Hou JY, Grant RA, Sauer RT, Baker TA Mol Cell. 2011 Jul 22;43(2):217-28. PMID:21777811<ref>PMID:21777811</ref>
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
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==See Also==
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</div>
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*[[ATP-dependent Clp protease adaptor protein 3D structures|ATP-dependent Clp protease adaptor protein 3D structures]]
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
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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: Hou, J Y.]]
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[[Category: Grant RA]]
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[[Category: Roman-Hernandez, G.]]
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[[Category: Hou JY]]
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[[Category: Sauer, R T.]]
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[[Category: Roman-Hernandez G]]
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[[Category: Adaptor]]
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[[Category: Sauer RT]]
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[[Category: Hydrolase]]
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Current revision

P1 crystal form of E. coli ClpS at 1.4 A resolution

PDB ID 3o1f

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