1e94

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[[Image:1e94.png|left|200px]]
 
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==HslV-HslU from E.coli==
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The line below this paragraph, containing "STRUCTURE_1e94", creates the "Structure Box" on the page.
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<StructureSection load='1e94' size='340' side='right'caption='[[1e94]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
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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'>[[1e94]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_BL21(DE3) Escherichia coli BL21(DE3)]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1doo 1doo]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1E94 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1E94 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]] 2.8&#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=ANP:PHOSPHOAMINOPHOSPHONIC+ACID-ADENYLATE+ESTER'>ANP</scene></td></tr>
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{{STRUCTURE_1e94| PDB=1e94 | SCENE= }}
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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=1e94 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1e94 OCA], [https://pdbe.org/1e94 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1e94 RCSB], [https://www.ebi.ac.uk/pdbsum/1e94 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1e94 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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== 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/e9/1e94_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=1e94 ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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HslVU is an ATP-dependent prokaryotic protease complex. Despite detailed crystal and molecular structure determinations of free HslV and HslU, the mechanism of ATP-dependent peptide and protein hydrolysis remained unclear, mainly because the productive complex of HslV and HslU could not be unambiguously identified from the crystal data. In the crystalline complex, the I domains of HslU interact with HslV. Observations based on electron microscopy data were interpreted in the light of the crystal structure to indicate an alternative mode of association with the intermediate domains away from HslV. By generation and analysis of two dozen HslU mutants, we find that the amidolytic and caseinolytic activities of HslVU are quite robust to mutations on both alternative docking surfaces on HslU. In contrast, HslVU activity against the maltose-binding protein-SulA fusion protein depends on the presence of the I domain and is also sensitive to mutations in the N-terminal and C-terminal domains of HslU. Mutational studies around the hexameric pore of HslU seem to show that it is involved in the recognition/translocation of maltose-binding protein-SulA but not of chromogenic small substrates and casein. ATP-binding site mutations, among other things, confirm the essential role of the "sensor arginine" (R393) and the "arginine finger" (R325) in the ATPase action of HslU and demonstrate an important role for E321. Additionally, we report a better refined structure of the HslVU complex crystallized along with resorufin-labeled casein.
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===HSLV-HSLU FROM E.COLI===
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Mutational studies on HslU and its docking mode with HslV.,Song HK, Hartmann C, Ramachandran R, Bochtler M, Behrendt R, Moroder L, Huber R Proc Natl Acad Sci U S A. 2000 Dec 19;97(26):14103-8. PMID:11114186<ref>PMID:11114186</ref>
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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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The line below this paragraph, {{ABSTRACT_PUBMED_11114186}}, adds the Publication Abstract to the page
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<div class="pdbe-citations 1e94" style="background-color:#fffaf0;"></div>
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(as it appears on PubMed at http://www.pubmed.gov), where 11114186 is the PubMed ID number.
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{{ABSTRACT_PUBMED_11114186}}
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==About this Structure==
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[[1e94]] is a 6 chain structure of [[Heat Shock Proteins]] with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1doo 1doo]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1E94 OCA].
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==See Also==
==See Also==
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*[[Heat Shock Proteins]]
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*[[Heat Shock Protein structures|Heat Shock Protein structures]]
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== References ==
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==Reference==
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<references/>
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<ref group="xtra">PMID:11114186</ref><ref group="xtra">PMID:10693812</ref><ref group="xtra">PMID:9177170</ref><ref group="xtra">PMID:8650174</ref><ref group="xtra">PMID:8244018</ref><references group="xtra"/>
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__TOC__
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[[Category: Escherichia coli]]
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</StructureSection>
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[[Category: Bochtler, M.]]
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[[Category: Large Structures]]
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[[Category: Hartmann, C.]]
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[[Category: Bochtler M]]
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[[Category: Ravishankar, R.]]
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[[Category: Hartmann C]]
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[[Category: Song, H K.]]
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[[Category: Ravishankar R]]
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[[Category: Aaa-atpase]]
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[[Category: Song HK]]
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[[Category: Atp-dependent proteolysis]]
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[[Category: Chaperone]]
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[[Category: Clpqy]]
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[[Category: Hslvu]]
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[[Category: Proteasome]]
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Current revision

HslV-HslU from E.coli

PDB ID 1e94

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