3o1f: Difference between revisions
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New page: '''Unreleased structure''' The entry 3o1f is ON HOLD Authors: Roman-Hernandez, G, Grant, RA, Sauer, RT, Baker, TA, de Regt, A Description: P1 crystal form of E. coli ClpS at 1.4 resolu... |
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The | ==P1 crystal form of E. coli ClpS at 1.4 A resolution== | ||
<StructureSection load='3o1f' size='340' side='right'caption='[[3o1f]], [[Resolution|resolution]] 1.40Å' scene=''> | |||
== Structural highlights == | |||
<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> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.4Å</td></tr> | |||
<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> | |||
<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> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/CLPS_ECOLI CLPS_ECOLI] 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 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. | |||
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> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 3o1f" 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__ | |||
</StructureSection> | |||
[[Category: Escherichia coli]] | |||
[[Category: Large Structures]] | |||
[[Category: Baker TA]] | |||
[[Category: Grant RA]] | |||
[[Category: Hou JY]] | |||
[[Category: Roman-Hernandez G]] | |||
[[Category: Sauer RT]] | |||
