2efg

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{{STRUCTURE_2efg| PDB=2efg | SCENE= }}
{{STRUCTURE_2efg| PDB=2efg | SCENE= }}
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'''TRANSLATIONAL ELONGATION FACTOR G COMPLEXED WITH GDP'''
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===TRANSLATIONAL ELONGATION FACTOR G COMPLEXED WITH GDP===
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==Overview==
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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.
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{{ABSTRACT_PUBMED_8070396}}
==About this Structure==
==About this Structure==
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[[Category: Translation]]
[[Category: Translation]]
[[Category: Translocase]]
[[Category: Translocase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 15:27:04 2008''

Revision as of 12:27, 28 July 2008

Image:2efg.png

Template:STRUCTURE 2efg

TRANSLATIONAL ELONGATION FACTOR G COMPLEXED WITH GDP

Template:ABSTRACT PUBMED 8070396

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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