3e76: Difference between revisions

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-[[Image:3e76.png|left|200px]]
-<!--
+==Crystal structure of Wild-type GroEL with bound Thallium ions==
-The line below this paragraph, containing "STRUCTURE_3e76", creates the "Structure Box" on the page.
+<StructureSection load='3e76' size='340' side='right'caption='[[3e76]], [[Resolution|resolution]] 3.94&Aring;' scene=''>
-You may change the PDB parameter (which sets the PDB file loaded into the applet)
+== Structural highlights ==
-or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
+<table><tr><td colspan='2'>[[3e76]] is a 14 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_UTI89 Escherichia coli UTI89]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3E76 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3E76 FirstGlance]. <br>
-or leave the SCENE parameter empty for the default display.
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.94&#8491;</td></tr>
--->
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=AGS:PHOSPHOTHIOPHOSPHORIC+ACID-ADENYLATE+ESTER'>AGS</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=TL:THALLIUM+(I)+ION'>TL</scene></td></tr>
-{{STRUCTURE_3e76|  PDB=3e76  |  SCENE=  }}
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3e76 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3e76 OCA], [https://pdbe.org/3e76 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3e76 RCSB], [https://www.ebi.ac.uk/pdbsum/3e76 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3e76 ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/CH60_ECOUT CH60_ECOUT] Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions (By similarity).
+== 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/e7/3e76_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=3e76 ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+GroEL is a bacterial chaperone protein that assembles into a homotetradecameric complex exhibiting D(7) symmetry and utilizes the co-chaperone protein GroES and ATP hydrolysis to assist in the proper folding of a variety of cytosolic proteins. GroEL utilizes two metal cofactors, Mg(2+) and K(+), to bind and hydrolyze ATP. A K(+)-binding site has been proposed to be located next to the nucleotide-binding site, but the available structural data do not firmly support this conclusion. Moreover, more than one functionally significant K(+)-binding site may exist within GroEL. Because K(+) has important and complex effects on GroEL activity and is involved in both positive (intra-ring) and negative (inter-ring) cooperativity for ATP hydrolysis, it is important to determine the exact location of these cation-binding site(s) within GroEL. In this study, the K(+) mimetic Tl(+) was incorporated into GroEL crystals, a moderately redundant 3.94 A resolution X-ray diffraction data set was collected from a single crystal and the strong anomalous scattering signal from the thallium ion was used to identify monovalent cation-binding sites. The results confirmed the previously proposed placement of K(+) next to the nucleotide-binding site and also identified additional binding sites that may be important for GroEL function and cooperativity. These findings also demonstrate the general usefulness of Tl(+) for the identification of monovalent cation-binding sites in protein crystal structures, even when the quality and resolution of the diffraction data are relatively low.
-===Crystal structure of Wild-type GroEL with bound Thallium ions===
+Use of thallium to identify monovalent cation binding sites in GroEL.,Kiser PD, Lorimer GH, Palczewski K Acta Crystallogr Sect F Struct Biol Cryst Commun. 2009 Oct 1;65(Pt, 10):967-71. Epub 2009 Sep 18. PMID:19851000<ref>PMID:19851000</ref>
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-<!--
+</div>
-The line below this paragraph, {{ABSTRACT_PUBMED_19851000}}, adds the Publication Abstract to the page
+<div class="pdbe-citations 3e76" style="background-color:#fffaf0;"></div>
-(as it appears on PubMed at http://www.pubmed.gov), where 19851000 is the PubMed ID number.
--->
-{{ABSTRACT_PUBMED_19851000}}
-==About this Structure==
-[[3e76]] is a 14 chain structure of [[Heat Shock Proteins]] with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli_uti89 Escherichia coli uti89]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3E76 OCA].
 ==See Also==
-*[[Heat Shock Proteins]]
+*[[Heat Shock Protein structures|Heat Shock Protein structures]]
+== References ==
-==Reference==
+<references/>
-<ref group="xtra">PMID:19851000</ref><references group="xtra"/>
+__TOC__
-[[Category: Chaperonin ATPase]]
+</StructureSection>
-[[Category: Escherichia coli uti89]]
+[[Category: Escherichia coli UTI89]]
-[[Category: Kiser, P D.]]
+[[Category: Large Structures]]
-[[Category: Lorimer, G H.]]
+[[Category: Kiser PD]]
-[[Category: Palczewski, K.]]
+[[Category: Lorimer GH]]
-[[Category: Atp-binding]]
+[[Category: Palczewski K]]
-[[Category: Chaperone]]
-[[Category: Chaperonin]]
-[[Category: Cytoplasm]]
-[[Category: Groel]]
-[[Category: Hsp60]]
-[[Category: Nucleotide-binding]]
-[[Category: Thallium]]