1oel: Difference between revisions
New page: left|200px<br /><applet load="1oel" size="450" color="white" frame="true" align="right" spinBox="true" caption="1oel, resolution 2.8Å" /> '''CONFORMATIONAL VARIAB... |
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[[Image:1oel.jpg|left|200px]]<br /><applet load="1oel" size=" | [[Image:1oel.jpg|left|200px]]<br /><applet load="1oel" size="350" color="white" frame="true" align="right" spinBox="true" | ||
caption="1oel, resolution 2.8Å" /> | caption="1oel, resolution 2.8Å" /> | ||
'''CONFORMATIONAL VARIABILITY IN THE REFINED STRUCTURE OF THE CHAPERONIN GROEL AT 2.8 ANGSTROM RESOLUTION'''<br /> | '''CONFORMATIONAL VARIABILITY IN THE REFINED STRUCTURE OF THE CHAPERONIN GROEL AT 2.8 ANGSTROM RESOLUTION'''<br /> | ||
==Overview== | ==Overview== | ||
Improved refinement of the crystal structure of GroEL from Escherichia | 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== | ==About this Structure== | ||
1OEL is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http:// | 1OEL is a [http://en.wikipedia.org/wiki/Single_protein 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== | ||
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[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Adams, P | [[Category: Adams, P D.]] | ||
[[Category: Braig, K.]] | [[Category: Braig, K.]] | ||
[[Category: Brunger, A | [[Category: Brunger, A T.]] | ||
[[Category: chaperonin]] | [[Category: chaperonin]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:16:50 2008'' | ||
Revision as of 15:16, 21 February 2008
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CONFORMATIONAL VARIABILITY IN THE REFINED STRUCTURE OF THE CHAPERONIN GROEL AT 2.8 ANGSTROM RESOLUTION
OverviewOverview
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 StructureAbout this Structure
1OEL is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
ReferenceReference
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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