1egs

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[[Image:1egs.jpg|left|200px]]
 
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==NMR STRUCTURE OF GROES MOBILE LOOP RESIDUES 19-27 IN THE SYNTHETIC PEPTIDE (RESIDUES 13-32) BOUND TO GROEL, 20 STRUCTURES==
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The line below this paragraph, containing "STRUCTURE_1egs", creates the "Structure Box" on the page.
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<StructureSection load='1egs' size='340' side='right'caption='[[1egs]]' 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'>[[1egs]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1EGS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1EGS 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">Solution NMR, 20 models</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=ACE:ACETYL+GROUP'>ACE</scene>, <scene name='pdbligand=NH2:AMINO+GROUP'>NH2</scene></td></tr>
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{{STRUCTURE_1egs| PDB=1egs | 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=1egs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1egs OCA], [https://pdbe.org/1egs PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1egs RCSB], [https://www.ebi.ac.uk/pdbsum/1egs PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1egs ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/CH10_ECOLI CH10_ECOLI] Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter.[HAMAP-Rule:MF_00580]
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Protein-protein interactions typically are characterized by highly specific interfaces that mediate binding with precisely tuned affinities. Binding of the Escherichia coli cochaperonin GroES to chaperonin GroEL is mediated, at least in part, by a mobile polypeptide loop in GroES that becomes immobilized in the GroEL/GroES/nucleotide complex. The bacteriophage T4 cochaperonin Gp31 possesses a similar highly flexible polypeptide loop in a region of the protein that shows low, but significant, amino acid similarity with GroES and other cochaperonins. When bound to GroEL, a synthetic peptide representing the mobile loop of either GroES or Gp31 adopts a characteristic bulged hairpin conformation as determined by transferred nuclear Overhauser effects in NMR spectra. Thermodynamic considerations suggest that flexible disorder in the cochaperonin mobile loops moderates their affinity for GroEL to facilitate cycles of chaperonin-mediated protein folding.
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'''NMR STRUCTURE OF GROES MOBILE LOOP RESIDUES 19-27 IN THE SYNTHETIC PEPTIDE (RESIDUES 13-32) BOUND TO GROEL, 20 STRUCTURES'''
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Interplay of structure and disorder in cochaperonin mobile loops.,Landry SJ, Taher A, Georgopoulos C, van der Vies SM Proc Natl Acad Sci U S A. 1996 Oct 15;93(21):11622-7. PMID:8876186<ref>PMID:8876186</ref>
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==Overview==
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Protein-protein interactions typically are characterized by highly specific interfaces that mediate binding with precisely tuned affinities. Binding of the Escherichia coli cochaperonin GroES to chaperonin GroEL is mediated, at least in part, by a mobile polypeptide loop in GroES that becomes immobilized in the GroEL/GroES/nucleotide complex. The bacteriophage T4 cochaperonin Gp31 possesses a similar highly flexible polypeptide loop in a region of the protein that shows low, but significant, amino acid similarity with GroES and other cochaperonins. When bound to GroEL, a synthetic peptide representing the mobile loop of either GroES or Gp31 adopts a characteristic bulged hairpin conformation as determined by transferred nuclear Overhauser effects in NMR spectra. Thermodynamic considerations suggest that flexible disorder in the cochaperonin mobile loops moderates their affinity for GroEL to facilitate cycles of chaperonin-mediated protein folding.
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==About this Structure==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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1EGS is a [[Single protein]] structure of sequence 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=1EGS OCA].
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</div>
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<div class="pdbe-citations 1egs" style="background-color:#fffaf0;"></div>
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==Reference==
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==See Also==
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Interplay of structure and disorder in cochaperonin mobile loops., Landry SJ, Taher A, Georgopoulos C, van der Vies SM, Proc Natl Acad Sci U S A. 1996 Oct 15;93(21):11622-7. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/8876186 8876186]
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*[[Chaperonin 3D structures|Chaperonin 3D structures]]
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== References ==
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<references/>
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__TOC__
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</StructureSection>
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Landry, S J.]]
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[[Category: Landry SJ]]
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[[Category: Chaperonin]]
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[[Category: Heat shock]]
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[[Category: Nmr]]
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[[Category: Protein folding]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 15:05:04 2008''
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Current revision

NMR STRUCTURE OF GROES MOBILE LOOP RESIDUES 19-27 IN THE SYNTHETIC PEPTIDE (RESIDUES 13-32) BOUND TO GROEL, 20 STRUCTURES

PDB ID 1egs

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