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="450" color="white" frame="true" align="right" spinBox="true"  
[[Image:1oel.jpg|left|200px]]<br /><applet load="1oel" size="350" color="white" frame="true" align="right" spinBox="true"  
caption="1oel, resolution 2.8&Aring;" />
caption="1oel, resolution 2.8&Aring;" />
'''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, 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.
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://ispc.weizmann.ac.il/oca-bin/ocashort?id=1OEL OCA].  
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.D.]]
[[Category: Adams, P D.]]
[[Category: Braig, K.]]
[[Category: Braig, K.]]
[[Category: Brunger, A.T.]]
[[Category: Brunger, A T.]]
[[Category: chaperonin]]
[[Category: chaperonin]]


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