1hqy: Difference between revisions

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-[[Image:1hqy.gif|left|200px]]
- {{Structure
+==Nucleotide-Dependent Conformational Changes in a Protease-Associated ATPase HslU==
-|PDB= 1hqy |SIZE=350|CAPTION= <scene name='initialview01'>1hqy</scene>, resolution 2.80&Aring;
+<StructureSection load='1hqy' size='340' side='right'caption='[[1hqy]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
-|SITE=
+== Structural highlights ==
-|LIGAND= <scene name='pdbligand=ADP:ADENOSINE-5&#39;-DIPHOSPHATE'>ADP</scene>
+<table><tr><td colspan='2'>[[1hqy]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_BL21(DE3) Escherichia coli BL21(DE3)]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HQY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1HQY FirstGlance]. <br>
-|ACTIVITY=
+</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>
-|GENE=
+<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></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=1hqy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1hqy OCA], [https://pdbe.org/1hqy PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1hqy RCSB], [https://www.ebi.ac.uk/pdbsum/1hqy PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1hqy ProSAT]</span></td></tr>
+</table>
+== Function ==
+[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>
+== Evolutionary Conservation ==
+[[Image:Consurf_key_small.gif|200px|right]]
+Check<jmol>
+  <jmolCheckbox>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/hq/1hqy_consurf.spt"</scriptWhenChecked>
+    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
+    <text>to colour the structure by Evolutionary Conservation</text>
+  </jmolCheckbox>
+</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=1hqy ConSurf].
+<div style="clear:both"></div>
-'''Nucleotide-Dependent Conformational Changes in a Protease-Associated ATPase HslU'''
+==See Also==
+*[[Heat Shock Protein structures|Heat Shock Protein structures]]
+== References ==
-==Overview==
+<references/>
-BACKGROUND: The bacterial heat shock locus ATPase HslU is an AAA(+) protein that has structures known in many nucleotide-free and -bound states. Nucleotide is required for the formation of the biologically active HslU hexameric assembly. The hexameric HslU ATPase binds the dodecameric HslV peptidase and forms an ATP-dependent HslVU protease. RESULTS: We have characterized four distinct HslU conformational states, going sequentially from open to closed: the empty, SO(4), ATP, and ADP states. The nucleotide binds at a cleft formed by an alpha/beta domain and an alpha-helical domain in HslU. The four HslU states differ by a rotation of the alpha-helical domain. This classification leads to a correction of nucleotide identity in one structure and reveals the ATP hydrolysis-dependent structural changes in the HslVU complex, including a ring rotation and a conformational change of the HslU C terminus. This leads to an amended protein unfolding-coupled translocation mechanism. CONCLUSIONS: The observed nucleotide-dependent conformational changes in HslU and their governing principles provide a framework for the mechanistic understanding of other AAA(+) proteins.
+__TOC__
+</StructureSection>
-==About this Structure==
+[[Category: Large Structures]]
-HQY is a [[Protein complex]] structure of sequences 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=1HQY OCA].
+[[Category: Chung CH]]
+[[Category: Eom SH]]
-==Reference==
+[[Category: Franklin MC]]
-Nucleotide-dependent conformational changes in a protease-associated ATPase HsIU., Wang J, Song JJ, Seong IS, Franklin MC, Kamtekar S, Eom SH, Chung CH, Structure. 2001 Nov;9(11):1107-16. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11709174 11709174]
+[[Category: Kamtekar S]]
-[[Category: Escherichia coli]]
+[[Category: Seong IS]]
-[[Category: Protein complex]]
+[[Category: Song JJ]]
-[[Category: Chung, C H.]]
+[[Category: Wang J]]
-[[Category: Eom, S H.]]
-[[Category: Franklin, M C.]]
-[[Category: Kamtekar, S.]]
-[[Category: Seong, I S.]]
-[[Category: Song, J J.]]
-[[Category: Wang, J.]]
-[[Category: ADP]]
-[[Category: hslvu]]
-[[Category: peptidase-atpase complex]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 23 12:07:15 2008''