1q2v

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[[Image:1q2v.jpg|left|200px]]
 
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==Crystal structure of the chaperonin from Thermococcus strain KS-1 (nucleotide-free form)==
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The line below this paragraph, containing "STRUCTURE_1q2v", creates the "Structure Box" on the page.
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<StructureSection load='1q2v' size='340' side='right'caption='[[1q2v]], [[Resolution|resolution]] 2.40&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'>[[1q2v]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermococcus_sp._JCM_11816 Thermococcus sp. JCM 11816]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Q2V OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1Q2V 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]] 2.4&#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=SO4:SULFATE+ION'>SO4</scene></td></tr>
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{{STRUCTURE_1q2v| PDB=1q2v | 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=1q2v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1q2v OCA], [https://pdbe.org/1q2v PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1q2v RCSB], [https://www.ebi.ac.uk/pdbsum/1q2v PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1q2v ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/THSA_THEK1 THSA_THEK1] Molecular chaperone; binds unfolded polypeptides in vitro, and has a weak ATPase activity.
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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/q2/1q2v_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=1q2v ConSurf].
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<div style="clear:both"></div>
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'''Crystal structure of the chaperonin from Thermococcus strain KS-1 (nucleotide-free form)'''
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==See Also==
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*[[Chaperonin 3D structures|Chaperonin 3D structures]]
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__TOC__
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==Overview==
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</StructureSection>
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The crystal structures of the group II chaperonins consisting of the alpha subunit with amino acid substitutions of G65C and/or I125T from the hyperthermophilic archaeum Thermococcus strain KS-1 were determined. These mutants have been shown to be active in ATP hydrolysis but inactive in protein folding. The structures were shown to be double-ring hexadecamers in an extremely closed form, which was consistent with the crystal structure of native alpha8beta8-chaperonin from Thermoplasma acidophilum. Comparisons of the present structures with the atomic structures of the GroEL14-GroES7-(ADP)7 complex revealed that the deficiency in protein-folding activity with the G65C amino acid substitution is caused by the steric hindrance of the local conformational change in an equatorial domain. We concluded that this mutant chaperonin with G65C substitution is deprived of the smooth conformational change in the refolding-reaction cycle. We obtained a new form of crystal with a distinct space group at a lower concentration of sulfate ion in the presence of nucleotide. The crystal structure obtained at the lower concentration of sulfate ion tilts outward, and has much looser inter-subunit contacts compared with those in the presence of a higher concentration of sulfate ion. Such subunit rotation has never been characterized in group II chaperonins. The crystal structure obtained at the lower concentration of sulfate ion tilts outward, and has much looser inter-subunit contacts compared with those in the presence of a higher concentration of sulfate ion.
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[[Category: Large Structures]]
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[[Category: Thermococcus sp. JCM 11816]]
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==About this Structure==
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[[Category: Iizuka R]]
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1Q2V is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Thermococcus_sp. Thermococcus sp.]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Q2V OCA].
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[[Category: Maruyama T]]
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[[Category: Miki K]]
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==Reference==
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[[Category: Shomura Y]]
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Crystal structures of the group II chaperonin from Thermococcus strain KS-1: steric hindrance by the substituted amino acid, and inter-subunit rearrangement between two crystal forms., Shomura Y, Yoshida T, Iizuka R, Maruyama T, Yohda M, Miki K, J Mol Biol. 2004 Jan 30;335(5):1265-78. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/14729342 14729342]
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[[Category: Yohda M]]
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[[Category: Chaperonin ATPase]]
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[[Category: Yoshida T]]
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[[Category: Single protein]]
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[[Category: Thermococcus sp.]]
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[[Category: Iizuka, R.]]
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[[Category: Maruyama, T.]]
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[[Category: Miki, K.]]
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[[Category: Shomura, Y.]]
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[[Category: Yohda, M.]]
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[[Category: Yoshida, T.]]
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[[Category: Closed state]]
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[[Category: Hexadecamer]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 05:47:46 2008''
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Current revision

Crystal structure of the chaperonin from Thermococcus strain KS-1 (nucleotide-free form)

PDB ID 1q2v

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