1elo

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(New page: 200px<br /><applet load="1elo" size="450" color="white" frame="true" align="right" spinBox="true" caption="1elo, resolution 2.8&Aring;" /> '''ELONGATION FACTOR G W...)
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[[Image:1elo.gif|left|200px]]<br /><applet load="1elo" size="450" color="white" frame="true" align="right" spinBox="true"
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[[Image:1elo.gif|left|200px]]<br /><applet load="1elo" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1elo, resolution 2.8&Aring;" />
caption="1elo, resolution 2.8&Aring;" />
'''ELONGATION FACTOR G WITHOUT NUCLEOTIDE'''<br />
'''ELONGATION FACTOR G WITHOUT NUCLEOTIDE'''<br />
==Overview==
==Overview==
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The crystal structure of Thermus thermophilus elongation factor G without, guanine nucleotide was determined to 2.85 A. This GTPase has five domains, with overall dimensions of 50 x 60 x 118 A. The GTP binding domain has a, core common to other GTPases with a unique subdomain which probably, functions as an intrinsic nucleotide exchange factor. Domains I and II are, homologous to elongation factor Tu and their arrangement, both with and, without GDP, is more similar to elongation factor Tu in complex with a GTP, analogue than with GDP. Domains III and V show structural similarities to, ribosomal proteins. Domain IV protrudes from the main body of the protein, and has an extraordinary topology with a left-handed cross-over connection, between two parallel beta-strands.
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The crystal structure of Thermus thermophilus elongation factor G without guanine nucleotide was determined to 2.85 A. This GTPase has five domains with overall dimensions of 50 x 60 x 118 A. The GTP binding domain has a core common to other GTPases with a unique subdomain which probably functions as an intrinsic nucleotide exchange factor. Domains I and II are homologous to elongation factor Tu and their arrangement, both with and without GDP, is more similar to elongation factor Tu in complex with a GTP analogue than with GDP. Domains III and V show structural similarities to ribosomal proteins. Domain IV protrudes from the main body of the protein and has an extraordinary topology with a left-handed cross-over connection between two parallel beta-strands.
==About this Structure==
==About this Structure==
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1ELO is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Thermus_thermophilus Thermus thermophilus]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1ELO OCA].
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1ELO is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Thermus_thermophilus Thermus thermophilus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ELO OCA].
==Reference==
==Reference==
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[[Category: Garber, M.]]
[[Category: Garber, M.]]
[[Category: Liljas, A.]]
[[Category: Liljas, A.]]
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[[Category: Svensson, L.A.]]
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[[Category: Svensson, L A.]]
[[Category: Zheltonosova, J.]]
[[Category: Zheltonosova, J.]]
[[Category: elongation factor]]
[[Category: elongation factor]]
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[[Category: ribosomal translocase]]
[[Category: ribosomal translocase]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 14:06:47 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:29:03 2008''

Revision as of 10:29, 21 February 2008


1elo, resolution 2.8Å

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ELONGATION FACTOR G WITHOUT NUCLEOTIDE

Overview

The crystal structure of Thermus thermophilus elongation factor G without guanine nucleotide was determined to 2.85 A. This GTPase has five domains with overall dimensions of 50 x 60 x 118 A. The GTP binding domain has a core common to other GTPases with a unique subdomain which probably functions as an intrinsic nucleotide exchange factor. Domains I and II are homologous to elongation factor Tu and their arrangement, both with and without GDP, is more similar to elongation factor Tu in complex with a GTP analogue than with GDP. Domains III and V show structural similarities to ribosomal proteins. Domain IV protrudes from the main body of the protein and has an extraordinary topology with a left-handed cross-over connection between two parallel beta-strands.

About this Structure

1ELO is a Single protein structure of sequence from Thermus thermophilus. Full crystallographic information is available from OCA.

Reference

Three-dimensional structure of the ribosomal translocase: elongation factor G from Thermus thermophilus., AEvarsson A, Brazhnikov E, Garber M, Zheltonosova J, Chirgadze Y, al-Karadaghi S, Svensson LA, Liljas A, EMBO J. 1994 Aug 15;13(16):3669-77. PMID:8070397

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