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Open data
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Basic information
Entry | Database: PDB / ID: 1elo | ||||||
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Title | ELONGATION FACTOR G WITHOUT NUCLEOTIDE | ||||||
![]() | ELONGATION FACTOR G | ||||||
![]() | ELONGATION FACTOR / RIBOSOMAL TRANSLOCASE / GTP BINDING PROTEIN / HYDROLASE | ||||||
Function / homology | ![]() ribosome disassembly / translation elongation factor activity / GTPase activity / GTP binding / cytosol Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() | ||||||
![]() | Aevarsson, A. / Brazhnikov, E. / Garber, M. / Zheltonosova, J. / Chirgadze, Yu. / Al-Karadaghi, S. / Svensson, L.A. / Liljas, A. | ||||||
![]() | ![]() Title: Three-dimensional structure of the ribosomal translocase: elongation factor G from Thermus thermophilus. Authors: A AEvarsson / E Brazhnikov / M Garber / J Zheltonosova / Y Chirgadze / S al-Karadaghi / L A Svensson / A Liljas / ![]() Abstract: 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 ...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. #1: ![]() Title: The Structure of Elongation Factor G in Complex with Gdp: Conformational Flexibility and Nucleotide Exchange Authors: Al-Karadaghi, S. / Aevarsson, A. / Zheltonosova, J. / Garber, M. / Liljas, A. #2: ![]() Title: Structure-Based Sequence Alignment of Elongation Factors TU and G with Related Gtpases Involved in Translation Authors: Aevarsson, A. #3: ![]() Title: Ribosomal Proteins and Elongation Factors Authors: Liljas, A. / Garber, M. #4: ![]() Title: The Crystal Structure of Elongation Factor G Complexed with Gdp, at 2.7 A Resolution Authors: Czworkowski, J. / Wang, J. / Steitz, T.A. / Moore, P.B. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 118.5 KB | Display | ![]() |
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PDB format | ![]() | 89.9 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 374.6 KB | Display | ![]() |
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Full document | ![]() | 431.6 KB | Display | |
Data in XML | ![]() | 20.4 KB | Display | |
Data in CIF | ![]() | 29.9 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Similar structure data |
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Links
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Assembly
Deposited unit | ![]()
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Unit cell |
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Components
#1: Protein | Mass: 76977.102 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() ![]() |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 3.03 Å3/Da / Density % sol: 59.38 % | ||||||||||||||||||||
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Crystal grow | *PLUS Temperature: 4 ℃ / Method: vapor diffusion, hanging drop / Details: Casale, E., (1991) J. Mol. Biol., 222, 447. / PH range low: 7 / PH range high: 4.4 | ||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction source | Wavelength: 1.5418 |
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Detector | Type: SIEMENS / Detector: AREA DETECTOR |
Radiation | Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | % possible obs: 87 % / Observed criterion σ(I): 3 |
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Processing
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Refinement | Resolution: 2.8→8 Å / σ(F): 0 Details: PLEASE NOTE THAT THE "EFFECTOR" REGION (RESIDUES 40 - 67) IS INVISIBLE AND DOMAIN III IS DISORDERED AND POORLY VISIBLE IN MAPS. ASSIGNMENT OF SEQUENCE AND THE MODEL OF DOMAIN III IS VERY ...Details: PLEASE NOTE THAT THE "EFFECTOR" REGION (RESIDUES 40 - 67) IS INVISIBLE AND DOMAIN III IS DISORDERED AND POORLY VISIBLE IN MAPS. ASSIGNMENT OF SEQUENCE AND THE MODEL OF DOMAIN III IS VERY UNCERTAIN (RESIDUES 400 - 475). TEMPERATURE FACTORS HAVE NOT BEEN REFINED AND SOLVENT MOLECULES HAVE NOT BEEN INCLUDED.
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Displacement parameters | Biso mean: 22.63 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.8→8 Å
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Software | *PLUS Name: ![]() | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement | *PLUS Rfactor obs: 0.23 / Rfactor Rfree: 0.32 / Rfactor Rwork: 0.23 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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