2mvm: Difference between revisions
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==Solution structure of eEF1Bdelta CAR domain== | ==Solution structure of eEF1Bdelta CAR domain== | ||
<StructureSection load='2mvm' size='340' side='right' caption='[[2mvm | <StructureSection load='2mvm' size='340' side='right'caption='[[2mvm]]' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2mvm]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2MVM OCA]. For a <b>guided tour on the structure components</b> use [ | <table><tr><td colspan='2'>[[2mvm]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2MVM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2MVM FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2mvm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2mvm OCA], [https://pdbe.org/2mvm PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2mvm RCSB], [https://www.ebi.ac.uk/pdbsum/2mvm PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2mvm ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[ | [https://www.uniprot.org/uniprot/EF1D_HUMAN EF1D_HUMAN] Isoform 1: EF-1-beta and EF-1-delta stimulate the exchange of GDP bound to EF-1-alpha to GTP, regenerating EF-1-alpha for another round of transfer of aminoacyl-tRNAs to the ribosome. Isoform 2: Regulates induction of heat-shock-responsive genes through association with heat shock transcription factors and direct DNA-binding at heat shock promoter elements (HSE). | ||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Translationally-controlled tumor protein (TCTP) is an abundant protein which is highly conserved in eukaryotes. However, its primary function is still not clear. Human TCTP interacts with the metazoan-specific eukaryotic elongation factor 1Bdelta (eEF1Bdelta) and inhibits its guanine nucleotide exchange factor (GEF) activity, but the structural mechanism remains unknown. The interaction between TCTP and eEF1Bdelta was investigated by NMR titration, structure determination, paramagnetic relaxation enhancement, site-directed mutagenesis, isothermal titration calorimetry, and HADDOCK docking. We first demonstrated that the catalytic GEF domain of eEF1Bdelta is not responsible for binding to TCTP, but rather a previously unnoticed central acidic region (CAR) domain in eEF1Bdelta. The mutagenesis data and the structural model of the TCTP-eEF1Bdelta CAR domain complex revealed the key binding residues. These residues are highly conserved in eukaryotic TCTPs and in eEF1B GEFs including the eukaryotically-conserved eEF1Balpha, implying the interaction may be conserved in all eukaryotes. Interactions were confirmed between TCTP and the eEF1Balpha CAR domain for human, fission yeast and unicellular photosynthetic microalga proteins, suggesting that involvement in protein translation through the conserved interaction with eEF1B represents a primary function of TCTP. | |||
Evolutionarily Conserved Binding of Translationally-Controlled Tumor Protein to Eukaryotic Elongation Factor 1B.,Wu H, Gong W, Yao X, Wang J, Perrett S, Feng Y J Biol Chem. 2015 Jan 29. pii: jbc.M114.628594. PMID:25635048<ref>PMID:25635048</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 2mvm" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Elongation factor 3D structures|Elongation factor 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Homo sapiens]] | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: | [[Category: Feng Y]] | ||
[[Category: | [[Category: Wu H]] | ||
Latest revision as of 09:11, 15 May 2024
Solution structure of eEF1Bdelta CAR domainSolution structure of eEF1Bdelta CAR domain
Structural highlights
FunctionEF1D_HUMAN Isoform 1: EF-1-beta and EF-1-delta stimulate the exchange of GDP bound to EF-1-alpha to GTP, regenerating EF-1-alpha for another round of transfer of aminoacyl-tRNAs to the ribosome. Isoform 2: Regulates induction of heat-shock-responsive genes through association with heat shock transcription factors and direct DNA-binding at heat shock promoter elements (HSE). Publication Abstract from PubMedTranslationally-controlled tumor protein (TCTP) is an abundant protein which is highly conserved in eukaryotes. However, its primary function is still not clear. Human TCTP interacts with the metazoan-specific eukaryotic elongation factor 1Bdelta (eEF1Bdelta) and inhibits its guanine nucleotide exchange factor (GEF) activity, but the structural mechanism remains unknown. The interaction between TCTP and eEF1Bdelta was investigated by NMR titration, structure determination, paramagnetic relaxation enhancement, site-directed mutagenesis, isothermal titration calorimetry, and HADDOCK docking. We first demonstrated that the catalytic GEF domain of eEF1Bdelta is not responsible for binding to TCTP, but rather a previously unnoticed central acidic region (CAR) domain in eEF1Bdelta. The mutagenesis data and the structural model of the TCTP-eEF1Bdelta CAR domain complex revealed the key binding residues. These residues are highly conserved in eukaryotic TCTPs and in eEF1B GEFs including the eukaryotically-conserved eEF1Balpha, implying the interaction may be conserved in all eukaryotes. Interactions were confirmed between TCTP and the eEF1Balpha CAR domain for human, fission yeast and unicellular photosynthetic microalga proteins, suggesting that involvement in protein translation through the conserved interaction with eEF1B represents a primary function of TCTP. Evolutionarily Conserved Binding of Translationally-Controlled Tumor Protein to Eukaryotic Elongation Factor 1B.,Wu H, Gong W, Yao X, Wang J, Perrett S, Feng Y J Biol Chem. 2015 Jan 29. pii: jbc.M114.628594. PMID:25635048[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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