1aip

From Proteopedia

(Difference between revisions)

Revision as of 13:39, 24 December 2014

EF-TU EF-TS COMPLEX FROM THERMUS THERMOPHILUS

Structural highlights

1aip is a 8 chain structure with sequence from Thermus thermophilus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Resources:	FirstGlance, OCA, RCSB, PDBsum

Function

[EFTU1_THETH] This protein promotes the GTP-dependent binding of aminoacyl-tRNA to the A-site of ribosomes during protein biosynthesis. [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.

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

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^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Wang Y, Jiang Y, Meyering-Voss M, Sprinzl M, Sigler PB. Crystal structure of the EF-Tu.EF-Ts complex from Thermus thermophilus. Nat Struct Biol. 1997 Aug;4(8):650-6. PMID:9253415

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 See Also
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1aip"

@@ Line 5: / Line 5: @@
 </td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1aip FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1aip OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1aip RCSB], [http://www.ebi.ac.uk/pdbsum/1aip PDBsum]</span></td></tr>
 </table>
+== Function ==
+[[http://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. [[http://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.
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]

1aip

From Proteopedia

Revision as of 13:39, 24 December 2014

EF-TU EF-TS COMPLEX FROM THERMUS THERMOPHILUS

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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