1oel

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{{STRUCTURE_1oel| PDB=1oel | SCENE= }}
{{STRUCTURE_1oel| PDB=1oel | SCENE= }}
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'''CONFORMATIONAL VARIABILITY IN THE REFINED STRUCTURE OF THE CHAPERONIN GROEL AT 2.8 ANGSTROM RESOLUTION'''
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===CONFORMATIONAL VARIABILITY IN THE REFINED STRUCTURE OF THE CHAPERONIN GROEL AT 2.8 ANGSTROM RESOLUTION===
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==Overview==
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Improved refinement of the crystal structure of GroEL from Escherichia coli has resulted in a complete atomic model for the first 524 residues. A new torsion-angle dynamics method and non-crystallographic symmetry restraints were used in the refinement. The model indicates that conformational variability exists due to rigid-body movements between the apical and intermediate domains of GroEL, resulting in deviations from strict seven-fold symmetry. The regions of the protein involved in polypeptide and GroES binding show unusually high B factors; these values may indicate mobility or discrete disorder. The variability of these regions may play a role in the ability of GroEL to bind a wide variety of substrates.
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(as it appears on PubMed at http://www.pubmed.gov), where 8846220 is the PubMed ID number.
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{{ABSTRACT_PUBMED_8846220}}
==About this Structure==
==About this Structure==
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[[Category: Brunger, A T.]]
[[Category: Brunger, A T.]]
[[Category: Chaperonin]]
[[Category: Chaperonin]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 03:44:58 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 15:26:04 2008''

Revision as of 12:26, 27 July 2008

Image:1oel.png

Template:STRUCTURE 1oel

CONFORMATIONAL VARIABILITY IN THE REFINED STRUCTURE OF THE CHAPERONIN GROEL AT 2.8 ANGSTROM RESOLUTION

Template:ABSTRACT PUBMED 8846220

About this Structure

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

Reference

Conformational variability in the refined structure of the chaperonin GroEL at 2.8 A resolution., Braig K, Adams PD, Brunger AT, Nat Struct Biol. 1995 Dec;2(12):1083-94. PMID:8846220

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