1aip

<table><tr><td colspan='2'>[[1aip]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/"flavobacterium_thermophilum"_yoshida_and_oshima_1971 "flavobacterium thermophilum" yoshida and oshima 1971]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AIP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1AIP FirstGlance]. <br>

</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1aip FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1aip OCA], [https://pdbe.org/1aip PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1aip RCSB], [https://www.ebi.ac.uk/pdbsum/1aip PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1aip ProSAT]</span></td></tr>

[[https://www.uniprot.org/uniprot/EFTU1_THETH EFTU1_THETH]] This protein promotes the GTP-dependent binding of aminoacyl-tRNA to the A-site of ribosomes during protein biosynthesis. [[https://www.uniprot.org/uniprot/EFTS_THET8 EFTS_THET8]] Associates with the EF-Tu.GDP complex and induces the exchange of GDP to GTP. It remains bound to the aminoacyl-tRNA.EF-Tu.GTP complex up to the GTP hydrolysis stage on the ribosome.

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== Publication Abstract from PubMed ==

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.

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<ref>PMID:9253415</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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== References ==

<references/>

[[Category: Flavobacterium thermophilum yoshida and oshima 1971]]

[[Category: Jiang, Y]]

[[Category: Meyering-Voss, M]]

[[Category: Sigler, P B]]

[[Category: Sprinzl, M]]

[[Category: Wang, Y]]

[[Category: Nucleotide exchange]]