2efg: Difference between revisions
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|PDB= 2efg |SIZE=350|CAPTION= <scene name='initialview01'>2efg</scene>, resolution 2.60Å | |PDB= 2efg |SIZE=350|CAPTION= <scene name='initialview01'>2efg</scene>, resolution 2.60Å | ||
|SITE= | |SITE= | ||
|LIGAND= <scene name='pdbligand=GDP:GUANOSINE-5'-DIPHOSPHATE'>GDP</scene> | |LIGAND= <scene name='pdbligand=GDP:GUANOSINE-5'-DIPHOSPHATE'>GDP</scene>, <scene name='pdbligand=UNK:UNKNOWN'>UNK</scene> | ||
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
|DOMAIN= | |||
|RELATEDENTRY= | |||
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2efg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2efg OCA], [http://www.ebi.ac.uk/pdbsum/2efg PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2efg RCSB]</span> | |||
}} | }} | ||
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[[Category: Steitz, T A.]] | [[Category: Steitz, T A.]] | ||
[[Category: Wang, J.]] | [[Category: Wang, J.]] | ||
[[Category: elongation]] | [[Category: elongation]] | ||
[[Category: elongation factor]] | [[Category: elongation factor]] | ||
[[Category: gtp binding]] | [[Category: gtp binding]] | ||
[[Category: gtpase]] | [[Category: gtpase]] | ||
[[Category: guanosine nucleotide binding]] | [[Category: guanosine nucleotide binding,]] | ||
[[Category: protein synt factor]] | [[Category: protein synt factor]] | ||
[[Category: ribosome]] | [[Category: ribosome]] | ||
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[[Category: translocase]] | [[Category: translocase]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 02:48:17 2008'' | ||
Revision as of 02:48, 31 March 2008
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| , resolution 2.60Å | |||||||
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| Ligands: | , | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
TRANSLATIONAL ELONGATION FACTOR G COMPLEXED WITH GDP
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
2EFG is a Single protein structure of sequence from Thermus thermophilus. 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
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