1grl

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(New page: 200px<br /><applet load="1grl" size="450" color="white" frame="true" align="right" spinBox="true" caption="1grl, resolution 2.8&Aring;" /> '''THE CRYSTAL STRUCTURE...)
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'''THE CRYSTAL STRUCTURE OF THE BACTERIAL CHAPERONIN GROEL AT 2.8 ANGSTROMS'''<br />
'''THE CRYSTAL STRUCTURE OF THE BACTERIAL CHAPERONIN GROEL AT 2.8 ANGSTROMS'''<br />
==Overview==
==Overview==
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The crystal structure of Escherichia coli GroEL shows a porous cylinder of, 14 subunits made of two nearly 7-fold rotationally symmetrical rings, stacked back-to-back with dyad symmetry. The subunits consist of three, domains: a large equatorial domain that forms the foundation of the, assembly at its waist and holds the rings together; a large loosely, structured apical domain that forms the ends of the cylinder; and a small, slender intermediate domain that connects the two, creating side windows., The three-dimensional structure places most of the mutationally defined, functional sites on the channel walls and its outward invaginations, and, at the ends of the cylinder.
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The crystal structure of Escherichia coli GroEL shows a porous cylinder of 14 subunits made of two nearly 7-fold rotationally symmetrical rings stacked back-to-back with dyad symmetry. The subunits consist of three domains: a large equatorial domain that forms the foundation of the assembly at its waist and holds the rings together; a large loosely structured apical domain that forms the ends of the cylinder; and a small slender intermediate domain that connects the two, creating side windows. The three-dimensional structure places most of the mutationally defined functional sites on the channel walls and its outward invaginations, and at the ends of the cylinder.
==About this Structure==
==About this Structure==
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1GRL 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=1GRL OCA].
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1GRL 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=1GRL OCA].
==Reference==
==Reference==
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[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Boisvert, D.C.]]
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[[Category: Boisvert, D C.]]
[[Category: Braig, K.]]
[[Category: Braig, K.]]
[[Category: Hegde, R.]]
[[Category: Hegde, R.]]
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[[Category: Horwich, A.L.]]
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[[Category: Horwich, A L.]]
[[Category: Joachimiak, A.]]
[[Category: Joachimiak, A.]]
[[Category: Otwinowski, Z.]]
[[Category: Otwinowski, Z.]]
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[[Category: Sigler, P.B.]]
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[[Category: Sigler, P B.]]
[[Category: chaperonin]]
[[Category: chaperonin]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 16:15:07 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:53:10 2008''

Revision as of 10:53, 21 February 2008


1grl, resolution 2.8Å

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THE CRYSTAL STRUCTURE OF THE BACTERIAL CHAPERONIN GROEL AT 2.8 ANGSTROMS

Overview

The crystal structure of Escherichia coli GroEL shows a porous cylinder of 14 subunits made of two nearly 7-fold rotationally symmetrical rings stacked back-to-back with dyad symmetry. The subunits consist of three domains: a large equatorial domain that forms the foundation of the assembly at its waist and holds the rings together; a large loosely structured apical domain that forms the ends of the cylinder; and a small slender intermediate domain that connects the two, creating side windows. The three-dimensional structure places most of the mutationally defined functional sites on the channel walls and its outward invaginations, and at the ends of the cylinder.

About this Structure

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

Reference

The crystal structure of the bacterial chaperonin GroEL at 2.8 A., Braig K, Otwinowski Z, Hegde R, Boisvert DC, Joachimiak A, Horwich AL, Sigler PB, Nature. 1994 Oct 13;371(6498):578-86. PMID:7935790

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