1elo: Difference between revisions

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[[Image:1elo.gif|left|200px]]
{{Seed}}
[[Image:1elo.png|left|200px]]


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{{STRUCTURE_1elo|  PDB=1elo  |  SCENE=  }}  
{{STRUCTURE_1elo|  PDB=1elo  |  SCENE=  }}  


'''ELONGATION FACTOR G WITHOUT NUCLEOTIDE'''
===ELONGATION FACTOR G WITHOUT NUCLEOTIDE===




==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.
The line below this paragraph, {{ABSTRACT_PUBMED_8070397}}, adds the Publication Abstract to the page
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{{ABSTRACT_PUBMED_8070397}}


==About this Structure==
==About this Structure==
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[[Category: Hydrolase]]
[[Category: Hydrolase]]
[[Category: Ribosomal translocase]]
[[Category: Ribosomal translocase]]
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Revision as of 21:56, 30 June 2008

File:1elo.png

Template:STRUCTURE 1elo

ELONGATION FACTOR G WITHOUT NUCLEOTIDE

Template:ABSTRACT PUBMED 8070397

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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