1efg: Difference between revisions
No edit summary |
No edit summary |
||
Line 1: | Line 1: | ||
[[Image:1efg.gif|left|200px]] | [[Image:1efg.gif|left|200px]] | ||
<!-- | |||
The line below this paragraph, containing "STRUCTURE_1efg", 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_1efg| PDB=1efg | SCENE= }} | |||
}} | |||
'''THE CRYSTAL STRUCTURE OF ELONGATION FACTOR G COMPLEXED WITH GDP, AT 2.7 ANGSTROMS RESOLUTION''' | '''THE CRYSTAL STRUCTURE OF ELONGATION FACTOR G COMPLEXED WITH GDP, AT 2.7 ANGSTROMS RESOLUTION''' | ||
Line 19: | Line 16: | ||
==About this Structure== | ==About this Structure== | ||
1EFG is a [[Single protein]] structure | 1EFG is a [[Single protein]] structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1EFG OCA]. | ||
==Reference== | ==Reference== | ||
Line 28: | Line 25: | ||
[[Category: Steitz, T A.]] | [[Category: Steitz, T A.]] | ||
[[Category: Wang, J.]] | [[Category: Wang, J.]] | ||
[[Category: | [[Category: Elongation factor]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 15:01:59 2008'' | |||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on |
Revision as of 15:02, 2 May 2008
THE CRYSTAL STRUCTURE OF ELONGATION FACTOR G COMPLEXED WITH GDP, AT 2.7 ANGSTROMS RESOLUTION
OverviewOverview
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 StructureAbout this Structure
1EFG is a Single protein structure. Full crystallographic information is available from OCA.
ReferenceReference
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 Fri May 2 15:01:59 2008