1aip: Difference between revisions
New page: left|200px<br /><applet load="1aip" size="450" color="white" frame="true" align="right" spinBox="true" caption="1aip, resolution 3.0Å" /> '''EF-TU EF-TS COMPLEX F... |
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[[Image:1aip.gif|left|200px]]<br /><applet load="1aip" size=" | [[Image:1aip.gif|left|200px]]<br /><applet load="1aip" size="350" color="white" frame="true" align="right" spinBox="true" | ||
caption="1aip, resolution 3.0Å" /> | caption="1aip, resolution 3.0Å" /> | ||
'''EF-TU EF-TS COMPLEX FROM THERMUS THERMOPHILUS'''<br /> | '''EF-TU EF-TS COMPLEX FROM THERMUS THERMOPHILUS'''<br /> | ||
==Overview== | ==Overview== | ||
In order to study nucleotide exchange mechanisms in GTP-binding proteins, we have determined the crystal structure of the complex formed by the | In order to study nucleotide exchange mechanisms in GTP-binding proteins, we have determined the crystal structure of the complex formed by the elongation factor Tu (EF-Tu) and its exchange factor Ts (EF-Ts) from Thermus thermophilus. The complex is a dyad symmetrical heterotetramer in which each EF-Tu, through a bipartite interface, interacts with two subunits of EF-Ts, explaining the need for a dimeric exchange factor. The architecture of the assembly is distinctly different from that of the corresponding heterodimeric E. coli complex, in which the monomeric E. coli EF-Ts remarkably forms essentially the same bipartite interface with EF-Tu through a sequence/structural repeat. GDP is released primarily by a Ts-induced peptide flip in the nucleotide binding pocket that disrupts hydrogen bonds to the phosphates and repositions the peptide carbonyl so as to sterically and electrostatically eject the GDP. The exchange mechanism may have useful implications for receptor-induced exchange in heterotrimeric G proteins. | ||
==About this Structure== | ==About this Structure== | ||
1AIP is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Thermus_thermophilus Thermus thermophilus]. Full crystallographic information is available from [http:// | 1AIP is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Thermus_thermophilus Thermus thermophilus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AIP OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: Jiang, Y.]] | [[Category: Jiang, Y.]] | ||
[[Category: Meyering-Voss, M.]] | [[Category: Meyering-Voss, M.]] | ||
[[Category: Sigler, P | [[Category: Sigler, P B.]] | ||
[[Category: Sprinzl, M.]] | [[Category: Sprinzl, M.]] | ||
[[Category: Wang, Y.]] | [[Category: Wang, Y.]] | ||
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[[Category: nucleotide exchange]] | [[Category: nucleotide exchange]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:44:57 2008'' | ||
Revision as of 12:44, 21 February 2008
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EF-TU EF-TS COMPLEX FROM THERMUS THERMOPHILUS
OverviewOverview
In order to study nucleotide exchange mechanisms in GTP-binding proteins, we have determined the crystal structure of the complex formed by the elongation factor Tu (EF-Tu) and its exchange factor Ts (EF-Ts) from Thermus thermophilus. The complex is a dyad symmetrical heterotetramer in which each EF-Tu, through a bipartite interface, interacts with two subunits of EF-Ts, explaining the need for a dimeric exchange factor. The architecture of the assembly is distinctly different from that of the corresponding heterodimeric E. coli complex, in which the monomeric E. coli EF-Ts remarkably forms essentially the same bipartite interface with EF-Tu through a sequence/structural repeat. GDP is released primarily by a Ts-induced peptide flip in the nucleotide binding pocket that disrupts hydrogen bonds to the phosphates and repositions the peptide carbonyl so as to sterically and electrostatically eject the GDP. The exchange mechanism may have useful implications for receptor-induced exchange in heterotrimeric G proteins.
About this StructureAbout this Structure
1AIP is a Protein complex structure of sequences from Thermus thermophilus. Full crystallographic information is available from OCA.
ReferenceReference
Crystal structure of the EF-Tu.EF-Ts complex from Thermus thermophilus., Wang Y, Jiang Y, Meyering-Voss M, Sprinzl M, Sigler PB, Nat Struct Biol. 1997 Aug;4(8):650-6. PMID:9253415
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