2efg
From Proteopedia
Line 1: | Line 1: | ||
[[Image:2efg.jpg|left|200px]] | [[Image:2efg.jpg|left|200px]] | ||
- | + | <!-- | |
- | + | The line below this paragraph, containing "STRUCTURE_2efg", creates the "Structure Box" on the page. | |
- | + | You may change the PDB parameter (which sets the PDB file loaded into the applet) | |
- | + | or the SCENE parameter (which sets the initial scene displayed when the page is loaded), | |
- | | | + | or leave the SCENE parameter empty for the default display. |
- | | | + | --> |
- | + | {{STRUCTURE_2efg| PDB=2efg | SCENE= }} | |
- | + | ||
- | + | ||
- | }} | + | |
'''TRANSLATIONAL ELONGATION FACTOR G COMPLEXED WITH GDP''' | '''TRANSLATIONAL ELONGATION FACTOR G COMPLEXED WITH GDP''' | ||
Line 29: | Line 26: | ||
[[Category: Steitz, T A.]] | [[Category: Steitz, T A.]] | ||
[[Category: Wang, J.]] | [[Category: Wang, J.]] | ||
- | [[Category: | + | [[Category: Elongation]] |
- | [[Category: | + | [[Category: Elongation factor]] |
- | [[Category: | + | [[Category: Gtp binding]] |
- | [[Category: | + | [[Category: Gtpase]] |
- | [[Category: | + | [[Category: Guanosine nucleotide binding]] |
- | [[Category: | + | [[Category: Protein synt factor]] |
- | [[Category: | + | [[Category: Ribosome]] |
- | [[Category: | + | [[Category: Translation]] |
- | [[Category: | + | [[Category: Translocase]] |
- | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 02:28:16 2008'' | |
- | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + |
Revision as of 23:28, 3 May 2008
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 Page seeded by OCA on Sun May 4 02:28:16 2008