1la1: Difference between revisions

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[[Image:1la1.gif|left|200px]]
{{Seed}}
[[Image:1la1.png|left|200px]]


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{{STRUCTURE_1la1|  PDB=1la1  |  SCENE=  }}  
{{STRUCTURE_1la1|  PDB=1la1  |  SCENE=  }}  


'''Gro-EL Fragment (Apical Domain) Comprising Residues 188-379'''
===Gro-EL Fragment (Apical Domain) Comprising Residues 188-379===




==Overview==
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Advances in understanding how GroEL binds to non-native proteins are reported. Conformational flexibility in the GroEL apical domain, which could account for the variety of substrates that GroEL binds, is illustrated by comparison of several independent crystallographic structures of apical domain constructs that show conformational plasticity in helices H and I. Additionally, ESI-MS indicates that apical domain constructs have co-populated conformations at neutral pH. To assess the ability of different apical domain conformers to bind co-chaperone and substrate, model peptides corresponding to the mobile loop of GroES and to helix D from rhodanese were studied. Analysis of apical domain-peptide complexes by ESI-MS indicates that only the folded or partially folded apical domain conformations form complexes that survive gas phase conditions. Fluorescence binding studies show that the apical domain can fully bind both peptides independently. No competition for binding was observed, suggesting the peptides have distinct apical domain-binding sites. Blocking the GroES-apical domain-binding site in GroEL rendered the chaperonin inactive in binding GroES and in assisting the folding of denatured rhodanese, but still capable of binding non-native proteins, supporting the conclusion that GroES and substrate proteins have, at least partially, distinct binding sites even in the intact GroEL tetradecamer.
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{{ABSTRACT_PUBMED_12065585}}


==About this Structure==
==About this Structure==
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[[Category: Molecular chaperone]]
[[Category: Molecular chaperone]]
[[Category: Protein folding]]
[[Category: Protein folding]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 23:42:46 2008''
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jul 2 12:05:02 2008''

Revision as of 09:05, 2 July 2008

File:1la1.png

Template:STRUCTURE 1la1

Gro-EL Fragment (Apical Domain) Comprising Residues 188-379

Template:ABSTRACT PUBMED 12065585

About this Structure

1LA1 is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.

Reference

Structural plasticity and noncovalent substrate binding in the GroEL apical domain. A study using electrospay ionization mass spectrometry and fluorescence binding studies., Ashcroft AE, Brinker A, Coyle JE, Weber F, Kaiser M, Moroder L, Parsons MR, Jager J, Hartl UF, Hayer-Hartl M, Radford SE, J Biol Chem. 2002 Sep 6;277(36):33115-26. Epub 2002 Jun 13. PMID:12065585

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