1ned

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[[Image:1ned.gif|left|200px]]
 
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==CRYSTAL STRUCTURE OF HSLV (CLPQ) AT 3.8 ANGSTROMS RESOLUTION==
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The line below this paragraph, containing "STRUCTURE_1ned", creates the "Structure Box" on the page.
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<StructureSection load='1ned' size='340' side='right'caption='[[1ned]], [[Resolution|resolution]] 3.80&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[1ned]] is a 3 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=1NED OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1NED FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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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]] 3.8&#8491;</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=1ned FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ned OCA], [https://pdbe.org/1ned PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ned RCSB], [https://www.ebi.ac.uk/pdbsum/1ned PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ned ProSAT]</span></td></tr>
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{{STRUCTURE_1ned| PDB=1ned | SCENE= }}
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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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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ne/1ned_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1ned ConSurf].
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<div style="clear:both"></div>
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'''CRYSTAL STRUCTURE OF HSLV (CLPQ) AT 3.8 ANGSTROMS RESOLUTION'''
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==See Also==
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*[[Heat Shock Protein structures|Heat Shock Protein structures]]
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== References ==
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==Overview==
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<references/>
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Heat shock locus V (HslV; also called ClpQ) is the proteolytic core of the ATP-dependent protease HslVU in Escherichia coli. It has sequence similarity with the beta-type subunits of the eukaryotic and archaebacterial proteasomes. Unlike these particles, which display 72-point symmetry, it is a dimer of hexamers with 62-point symmetry. The crystal structure of HslV at 3.8-A resolution, determined by isomorphous replacement and symmetry averaging, shows that in spite of the different symmetry of the particle, the fold and the contacts between subunits are conserved. A tripeptide aldehyde inhibitor, acetyl-Leu-Leu-norleucinal, binds to the N-terminal threonine residue of HslV, probably as a hemiacetal, relating HslV also functionally to the proteasomes of archaea and eukaryotes.
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__TOC__
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</StructureSection>
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==About this Structure==
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1NED is a [[Single protein]] structure of 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=1NED OCA].
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==Reference==
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Crystal structure of heat shock locus V (HslV) from Escherichia coli., Bochtler M, Ditzel L, Groll M, Huber R, Proc Natl Acad Sci U S A. 1997 Jun 10;94(12):6070-4. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/9177170 9177170]
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[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Bochtler, M.]]
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[[Category: Bochtler M]]
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[[Category: Ditzel, L.]]
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[[Category: Ditzel L]]
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[[Category: Groll, M.]]
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[[Category: Groll M]]
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[[Category: Huber, R.]]
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[[Category: Huber R]]
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[[Category: Atp-dependent protease]]
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[[Category: Clpq]]
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[[Category: Clpqy]]
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[[Category: Hslv]]
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[[Category: Hslvu]]
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[[Category: Hydrolase]]
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[[Category: Proteasome]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 02:25:58 2008''
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Current revision

CRYSTAL STRUCTURE OF HSLV (CLPQ) AT 3.8 ANGSTROMS RESOLUTION

PDB ID 1ned

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