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| | <StructureSection load='4pc1' size='340' side='right'caption='[[4pc1]], [[Resolution|resolution]] 1.95Å' scene=''> | | <StructureSection load='4pc1' size='340' side='right'caption='[[4pc1]], [[Resolution|resolution]] 1.95Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4pc1]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895] and [http://en.wikipedia.org/wiki/Ecodh Ecodh]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4PC1 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4PC1 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4pc1]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] and [https://en.wikipedia.org/wiki/Escherichia_coli_str._K-12_substr._DH10B Escherichia coli str. K-12 substr. DH10B]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4PC1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4PC1 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=PB:LEAD+(II)+ION'>PB</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene>, <scene name='pdbligand=TRS:2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>TRS</scene></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=PB:LEAD+(II)+ION'>PB</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene>, <scene name='pdbligand=TRS:2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>TRS</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">tufA, tuf, ECDH10B_3514 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=316385 ECODH]), tsf, BN17_45931, ECs0172, LF82_2325 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 "Bacillus coli" Migula 1895])</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=4pc1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4pc1 OCA], [https://pdbe.org/4pc1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4pc1 RCSB], [https://www.ebi.ac.uk/pdbsum/4pc1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4pc1 ProSAT]</span></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=4pc1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4pc1 OCA], [http://pdbe.org/4pc1 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4pc1 RCSB], [http://www.ebi.ac.uk/pdbsum/4pc1 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4pc1 ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/B1X6I9_ECODH B1X6I9_ECODH]] This protein promotes the GTP-dependent binding of aminoacyl-tRNA to the A-site of ribosomes during protein biosynthesis.[HAMAP-Rule:MF_00118] [[http://www.uniprot.org/uniprot/C3TPM7_ECOLX C3TPM7_ECOLX]] 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.[HAMAP-Rule:MF_00050][RuleBase:RU000642] | + | [https://www.uniprot.org/uniprot/A0A0M3KKV1_ECODH A0A0M3KKV1_ECODH] This protein promotes the GTP-dependent binding of aminoacyl-tRNA to the A-site of ribosomes during protein biosynthesis.[HAMAP-Rule:MF_00118] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | ==See Also== | | ==See Also== |
| - | *[[Elongation factor|Elongation factor]] | + | *[[Elongation factor 3D structures|Elongation factor 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Bacillus coli migula 1895]] | + | [[Category: Escherichia coli]] |
| - | [[Category: Ecodh]] | + | [[Category: Escherichia coli str. K-12 substr. DH10B]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Thirup, S S]] | + | [[Category: Thirup SS]] |
| - | [[Category: Elongation factor]]
| + | |
| - | [[Category: G:gef complex]]
| + | |
| - | [[Category: Protein synthesis]]
| + | |
| - | [[Category: Translation]]
| + | |
| Structural highlights
Function
A0A0M3KKV1_ECODH This protein promotes the GTP-dependent binding of aminoacyl-tRNA to the A-site of ribosomes during protein biosynthesis.[HAMAP-Rule:MF_00118]
Publication Abstract from PubMed
Translation elongation factor EF-Tu belongs to the superfamily of guanine-nucleotide binding proteins, which play key cellular roles as regulatory switches. All G-proteins require activation via exchange of GDP for GTP to carry out their respective tasks. Often, guanine-nucleotide exchange factors are essential to this process. During translation, EF-Tu:GTP transports aminoacylated tRNA to the ribosome. GTP is hydrolyzed during this process, and subsequent reactivation of EF-Tu is catalyzed by EF-Ts. The reaction path of guanine-nucleotide exchange is structurally poorly defined for EF-Tu and EF-Ts. We have determined the crystal structures of the following reaction intermediates: two structures of EF-Tu:GDP:EF-Ts (2.2 and 1.8A resolution), EF-Tu:PO4:EF-Ts (1.9A resolution), EF-Tu:GDPNP:EF-Ts (2.2A resolution) and EF-Tu:GDPNP:pulvomycin:Mg2+:EF-Ts (3.5A resolution). These structures provide snapshots throughout the entire exchange reaction and suggest a mechanism for the release of EF-Tu in its GTP conformation. An inferred sequence of events during the exchange reaction is presented.
Structural outline of the detailed mechanism for elongation factor Ts-mediated guanine nucleotide exchange on elongation factor Tu.,Thirup SS, Van LB, Nielsen TK, Knudsen CR J Struct Biol. 2015 Jun 11. pii: S1047-8477(15)30015-0. doi:, 10.1016/j.jsb.2015.06.011. PMID:26073967[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Thirup SS, Van LB, Nielsen TK, Knudsen CR. Structural outline of the detailed mechanism for elongation factor Ts-mediated guanine nucleotide exchange on elongation factor Tu. J Struct Biol. 2015 Jun 11. pii: S1047-8477(15)30015-0. doi:, 10.1016/j.jsb.2015.06.011. PMID:26073967 doi:http://dx.doi.org/10.1016/j.jsb.2015.06.011
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