3k1j

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{{STRUCTURE_3k1j| PDB=3k1j | SCENE= }}
 
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===Crystal structure of Lon protease from Thermococcus onnurineus NA1===
 
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{{ABSTRACT_PUBMED_020834233}}
 
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==About this Structure==
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==Crystal structure of Lon protease from Thermococcus onnurineus NA1==
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[[3k1j]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Thermococcus_onnurineus Thermococcus onnurineus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3K1J OCA].
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<StructureSection load='3k1j' size='340' side='right'caption='[[3k1j]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
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[[Category: Thermococcus onnurineus]]
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== Structural highlights ==
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[[Category: An, Y J.]]
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<table><tr><td colspan='2'>[[3k1j]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermococcus_onnurineus_NA1 Thermococcus onnurineus NA1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3K1J OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3K1J FirstGlance]. <br>
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[[Category: Cha, S S.]]
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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&#8491;</td></tr>
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[[Category: Atp-binding]]
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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=PE4:2-{2-[2-(2-{2-[2-(2-ETHOXY-ETHOXY)-ETHOXY]-ETHOXY}-ETHOXY)-ETHOXY]-ETHOXY}-ETHANOL'>PE4</scene>, <scene name='pdbligand=PE8:3,6,9,12,15,18,21-HEPTAOXATRICOSANE-1,23-DIOL'>PE8</scene></td></tr>
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[[Category: Atp-dependent protease]]
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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=3k1j FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3k1j OCA], [https://pdbe.org/3k1j PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3k1j RCSB], [https://www.ebi.ac.uk/pdbsum/3k1j PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3k1j ProSAT]</span></td></tr>
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[[Category: Hydrolase]]
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</table>
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[[Category: Nucleotide-binding]]
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== Function ==
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[[Category: Protease]]
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[https://www.uniprot.org/uniprot/B6YU74_THEON B6YU74_THEON]
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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/k1/3k1j_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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=3k1j 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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Lon proteases are distributed in all kingdoms of life and are required for survival of cells under stress. Lon is a tandem fusion of an AAA+ molecular chaperone and a protease with a serine-lysine catalytic dyad. We report the 2.0-A resolution crystal structure of Thermococcus onnurineus NA1 Lon (TonLon). The structure is a three-tiered hexagonal cylinder with a large sequestered chamber accessible through an axial channel. Conserved loops extending from the AAA+ domain combine with an insertion domain containing the membrane anchor to form an apical domain that serves as a gate governing substrate access to an internal unfolding and degradation chamber. Alternating AAA+ domains are in tight- and weak-binding nucleotide states with different domain orientations and intersubunit contacts, reflecting intramolecular dynamics during ATP-driven protein unfolding and translocation. The bowl-shaped proteolytic chamber is contiguous with the chaperone chamber allowing internalized proteins direct access to the proteolytic sites without further gating restrictions.
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Crystal structure of Lon protease: molecular architecture of gated entry to a sequestered degradation chamber.,Cha SS, An YJ, Lee CR, Lee HS, Kim YG, Kim SJ, Kwon KK, De Donatis GM, Lee JH, Maurizi MR, Kang SG EMBO J. 2010 Oct 20;29(20):3520-30. Epub 2010 Sep 10. PMID:20834233<ref>PMID:20834233</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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<div class="pdbe-citations 3k1j" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Large Structures]]
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[[Category: Thermococcus onnurineus NA1]]
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[[Category: An YJ]]
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[[Category: Cha SS]]

Current revision

Crystal structure of Lon protease from Thermococcus onnurineus NA1

PDB ID 3k1j

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