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2efg

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|PDB= 2efg |SIZE=350|CAPTION= <scene name='initialview01'>2efg</scene>, resolution 2.60&Aring;
|PDB= 2efg |SIZE=350|CAPTION= <scene name='initialview01'>2efg</scene>, resolution 2.60&Aring;
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|LIGAND= <scene name='pdbligand=GDP:GUANOSINE-5'-DIPHOSPHATE'>GDP</scene>
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|LIGAND= <scene name='pdbligand=GDP:GUANOSINE-5&#39;-DIPHOSPHATE'>GDP</scene>
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[[Category: translocase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 16:39:23 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 23 15:00:40 2008''

Revision as of 13:00, 23 March 2008


PDB ID 2efg

Drag the structure with the mouse to rotate
, resolution 2.60Å
Ligands:
Coordinates: save as pdb, mmCIF, xml



TRANSLATIONAL ELONGATION FACTOR G COMPLEXED WITH GDP


Overview

Elongation factor G (EF-G) catalyzes the translocation step of protein synthesis in bacteria, and like the other bacterial elongation factor, EF-Tu--whose structure is already known--it is a member of the GTPase superfamily. We have determined the crystal structure of EF-G--GDP from Thermus thermophilus. It is an elongated molecule whose large, N-terminal domain resembles the G domain of EF-Tu, except for a 90 residue insert, which covers a surface that is involved in nucleotide exchange in EF-Tu and other G proteins. The tertiary structures of the second domains of EF-G and EF-Tu are nearly identical, but the relative placement of the first two domains in EF-G--GDP resembles that seen in EF-Tu--GTP, not EF-Tu--GDP. The remaining three domains of EF-G look like RNA binding domains, and have no counterparts in EF-Tu.

About this Structure

2EFG is a Single protein structure of sequence from Thermus thermophilus. Full crystallographic information is available from OCA.

Reference

The crystal structure of elongation factor G complexed with GDP, at 2.7 A resolution., Czworkowski J, Wang J, Steitz TA, Moore PB, EMBO J. 1994 Aug 15;13(16):3661-8. PMID:8070396

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