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1elo
From Proteopedia
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| - | [[Image:1elo.gif|left|200px]] | + | [[Image:1elo.gif|left|200px]] |
| - | + | ||
| - | '''ELONGATION FACTOR G WITHOUT NUCLEOTIDE''' | + | {{Structure |
| + | |PDB= 1elo |SIZE=350|CAPTION= <scene name='initialview01'>1elo</scene>, resolution 2.8Å | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''ELONGATION FACTOR G WITHOUT NUCLEOTIDE''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1ELO is a [ | + | 1ELO is a [[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== | ||
| - | 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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/8070397 8070397] |
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Thermus thermophilus]] | [[Category: Thermus thermophilus]] | ||
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[[Category: ribosomal translocase]] | [[Category: ribosomal translocase]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:57:25 2008'' |
Revision as of 08:57, 20 March 2008
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| , resolution 2.8Å | |||||||
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| 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
Page seeded by OCA on Thu Mar 20 10:57:25 2008
