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1efg
From Proteopedia
(New page: 200px<br /><applet load="1efg" size="450" color="white" frame="true" align="right" spinBox="true" caption="1efg, resolution 2.7Å" /> '''THE CRYSTAL STRUCTURE...) |
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| - | [[Image:1efg.gif|left|200px]]<br /><applet load="1efg" size=" | + | [[Image:1efg.gif|left|200px]]<br /><applet load="1efg" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1efg, resolution 2.7Å" /> | caption="1efg, resolution 2.7Å" /> | ||
'''THE CRYSTAL STRUCTURE OF ELONGATION FACTOR G COMPLEXED WITH GDP, AT 2.7 ANGSTROMS RESOLUTION'''<br /> | '''THE CRYSTAL STRUCTURE OF ELONGATION FACTOR G COMPLEXED WITH GDP, AT 2.7 ANGSTROMS RESOLUTION'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Elongation factor G (EF-G) catalyzes the translocation step of protein | + | 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== | ==About this Structure== | ||
| - | 1EFG is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/ ] with GDP as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | + | 1EFG is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/ ] with <scene name='pdbligand=GDP:'>GDP</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1EFG OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Czworkowski, J.]] | [[Category: Czworkowski, J.]] | ||
| - | [[Category: Moore, P | + | [[Category: Moore, P B.]] |
| - | [[Category: Steitz, T | + | [[Category: Steitz, T A.]] |
[[Category: Wang, J.]] | [[Category: Wang, J.]] | ||
[[Category: GDP]] | [[Category: GDP]] | ||
[[Category: elongation factor]] | [[Category: elongation factor]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:27:07 2008'' |
Revision as of 10:27, 21 February 2008
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THE CRYSTAL STRUCTURE OF ELONGATION FACTOR G COMPLEXED WITH GDP, AT 2.7 ANGSTROMS RESOLUTION
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
1EFG is a Single protein structure of sequence from [1] with as ligand. 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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