1egs: Difference between revisions

Revision as of 13:27, 21 February 2008

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

OverviewOverview

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.

About this StructureAbout this Structure

1EGS is a Single protein structure of sequence from Escherichia coli with and as ligands. Full crystallographic information is available from OCA.

ReferenceReference

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

Page seeded by OCA on Thu Feb 21 12:27:46 2008

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OCA

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-[[Image:1egs.jpg|left|200px]]<br /><applet load="1egs" size="450" color="white" frame="true" align="right" spinBox="true"
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 caption="1egs" />
 '''NMR STRUCTURE OF GROES MOBILE LOOP RESIDUES 19-27 IN THE SYNTHETIC PEPTIDE (RESIDUES 13-32) BOUND TO GROEL, 20 STRUCTURES'''<br />
 ==Overview==
-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.
+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.
 ==About this Structure==
-EGS is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with ACE and NH2 as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1EGS OCA].
+EGS is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with <scene name='pdbligand=ACE:'>ACE</scene> and <scene name='pdbligand=NH2:'>NH2</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1EGS OCA].
 ==Reference==
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 [[Category: Escherichia coli]]
 [[Category: Single protein]]
-[[Category: Landry, S.J.]]
+[[Category: Landry, S J.]]
 [[Category: ACE]]
 [[Category: NH2]]
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 [[Category: protein folding]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 13:59:46 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:27:46 2008''