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1elo
From Proteopedia
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[[Image:1elo.gif|left|200px]] | [[Image:1elo.gif|left|200px]] | ||
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'''ELONGATION FACTOR G WITHOUT NUCLEOTIDE''' | '''ELONGATION FACTOR G WITHOUT NUCLEOTIDE''' | ||
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[[Category: Svensson, L A.]] | [[Category: Svensson, L A.]] | ||
[[Category: Zheltonosova, J.]] | [[Category: Zheltonosova, J.]] | ||
| - | [[Category: | + | [[Category: Elongation factor]] |
| - | [[Category: | + | [[Category: Gtp binding protein]] |
| - | [[Category: | + | [[Category: Hydrolase]] |
| - | [[Category: | + | [[Category: Ribosomal translocase]] |
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Revision as of 12:15, 2 May 2008
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 Page seeded by OCA on Fri May 2 15:15:11 2008
