1oel
From Proteopedia
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| - | [[Image:1oel.jpg|left|200px]] | + | [[Image:1oel.jpg|left|200px]] |
| - | + | ||
| - | '''CONFORMATIONAL VARIABILITY IN THE REFINED STRUCTURE OF THE CHAPERONIN GROEL AT 2.8 ANGSTROM RESOLUTION''' | + | {{Structure |
| + | |PDB= 1oel |SIZE=350|CAPTION= <scene name='initialview01'>1oel</scene>, resolution 2.8Å | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= | ||
| + | |GENE= GROEL ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli]) | ||
| + | }} | ||
| + | |||
| + | '''CONFORMATIONAL VARIABILITY IN THE REFINED STRUCTURE OF THE CHAPERONIN GROEL AT 2.8 ANGSTROM RESOLUTION''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1OEL is a [ | + | 1OEL 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=1OEL OCA]. |
==Reference== | ==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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/8846220 8846220] |
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: chaperonin]] | [[Category: chaperonin]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 13:09:46 2008'' |
Revision as of 11:09, 20 March 2008
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| , resolution 2.8Å | |||||||
|---|---|---|---|---|---|---|---|
| Gene: | GROEL (Escherichia coli) | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
CONFORMATIONAL VARIABILITY IN THE REFINED STRUCTURE OF THE CHAPERONIN GROEL AT 2.8 ANGSTROM RESOLUTION
Overview
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.
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
Page seeded by OCA on Thu Mar 20 13:09:46 2008
