6pxi

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'''Unreleased structure'''
 
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The entry 6pxi is ON HOLD until Paper Publication
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==The crystal structure of a singly capped HslUV complex with an axial pore plug and a HslU E257Q mutation==
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<StructureSection load='6pxi' size='340' side='right'caption='[[6pxi]], [[Resolution|resolution]] 3.45&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[6pxi]] is a 6 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=6PXI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6PXI FirstGlance]. <br>
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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]] 3.447&#8491;</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=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></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=6pxi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6pxi OCA], [https://pdbe.org/6pxi PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6pxi RCSB], [https://www.ebi.ac.uk/pdbsum/6pxi PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6pxi ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/HSLV_ECOLI HSLV_ECOLI] Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. The complex has been shown to be involved in the specific degradation of heat shock induced transcription factors such as RpoH and SulA. In addition, small hydrophobic peptides are also hydrolyzed by HslV. HslV has weak protease activity even in the absence of HslU, but this activity is induced more than 100-fold in the presence of HslU. HslU recognizes protein substrates and unfolds these before guiding them to HslV for hydrolysis. HslV is not believed to degrade folded proteins.<ref>PMID:8662828</ref> <ref>PMID:8650174</ref> <ref>PMID:9288941</ref> <ref>PMID:9393683</ref> <ref>PMID:10452560</ref> <ref>PMID:10419524</ref> <ref>PMID:15696175</ref>
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Authors: Baytshtok, V., Grant, R.A., Sauer, R.T.
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==See Also==
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*[[ATPase 3D structures|ATPase 3D structures]]
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Description: The crystal structure of a singly capped HslUV complex with an axial pore plug and a HslU E257Q mutation
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*[[Heat Shock Protein structures|Heat Shock Protein structures]]
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[[Category: Unreleased Structures]]
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== References ==
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[[Category: Baytshtok, V]]
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<references/>
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[[Category: Sauer, R.T]]
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__TOC__
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[[Category: Grant, R.A]]
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</StructureSection>
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[[Category: Escherichia coli]]
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[[Category: Large Structures]]
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[[Category: Baytshtok V]]
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[[Category: Grant RA]]
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[[Category: Sauer RT]]

Current revision

The crystal structure of a singly capped HslUV complex with an axial pore plug and a HslU E257Q mutation

PDB ID 6pxi

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