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1elo
From Proteopedia
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|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1elo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1elo OCA], [http://www.ebi.ac.uk/pdbsum/1elo PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1elo RCSB]</span> | ||
}} | }} | ||
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[[Category: ribosomal translocase]] | [[Category: ribosomal translocase]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 20:05:05 2008'' |
Revision as of 17:05, 30 March 2008
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| , resolution 2.8Å | |||||||
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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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