This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.

1aip

From Proteopedia

(Difference between revisions)

Jump to: navigation, search

Revision as of 23:37, 9 September 2015

EF-TU EF-TS COMPLEX FROM THERMUS THERMOPHILUS

Structural highlights

1aip is a 8 chain structure with sequence from "flavobacterium_thermophilum"_yoshida_and_oshima_1971 "flavobacterium thermophilum" yoshida and oshima 1971. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Resources:	FirstGlance, OCA, PDBe, 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 2: / Line 2: @@
 <StructureSection load='1aip' size='340' side='right' caption='[[1aip]], [[Resolution|resolution]] 3.00&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1aip]] is a 8 chain structure with sequence 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]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1AIP FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1aip]] is a 8 chain structure with sequence from [http://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 [http://oca.weizmann.ac.il/oca-docs/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'>[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>
+</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://pdbe.org/1aip PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1aip RCSB], [http://www.ebi.ac.uk/pdbsum/1aip PDBsum]</span></td></tr>
 </table>
 == Function ==
@@ Line 25: / Line 25: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 1aip" style="background-color:#fffaf0;"></div>
 ==See Also==
@@ Line 32: / Line 33: @@
 __TOC__
 </StructureSection>
-[[Category: Thermus thermophilus]]
+[[Category: Flavobacterium thermophilum yoshida and oshima 1971]]
 [[Category: Jiang, Y]]
 [[Category: Meyering-Voss, M]]

1aip

From Proteopedia

Revision as of 23:37, 9 September 2015

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?)

Views

Personal tools

Navigation

Search

Toolbox