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5w75

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==Crystal Structure of Reconstructed Bacterial Elongation Factor Node 168==
==Crystal Structure of Reconstructed Bacterial Elongation Factor Node 168==
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<StructureSection load='5w75' size='340' side='right' caption='[[5w75]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
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<StructureSection load='5w75' size='340' side='right'caption='[[5w75]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[5w75]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5W75 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5W75 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[5w75]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermotoga_neapolitana_DSM_4359 Thermotoga neapolitana DSM 4359]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5W75 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5W75 FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GDP:GUANOSINE-5-DIPHOSPHATE'>GDP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=SUC:SUCROSE'>SUC</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.298&#8491;</td></tr>
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<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=5w75 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5w75 OCA], [http://pdbe.org/5w75 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5w75 RCSB], [http://www.ebi.ac.uk/pdbsum/5w75 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5w75 ProSAT]</span></td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FRU:FRUCTOSE'>FRU</scene>, <scene name='pdbligand=GDP:GUANOSINE-5-DIPHOSPHATE'>GDP</scene>, <scene name='pdbligand=GLC:ALPHA-D-GLUCOSE'>GLC</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=PRD_900003:sucrose'>PRD_900003</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5w75 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5w75 OCA], [https://pdbe.org/5w75 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5w75 RCSB], [https://www.ebi.ac.uk/pdbsum/5w75 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5w75 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/EFTU_THENN EFTU_THENN]] This protein promotes the GTP-dependent binding of aminoacyl-tRNA to the A-site of ribosomes during protein biosynthesis.[HAMAP-Rule:MF_00118]
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[https://www.uniprot.org/uniprot/EFTU_THENN EFTU_THENN] This protein promotes the GTP-dependent binding of aminoacyl-tRNA to the A-site of ribosomes during protein biosynthesis.[HAMAP-Rule:MF_00118]
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Rationally engineering thermostability in proteins would create enzymes and receptors that function under harsh industrial applications. Several sequence-based approaches can generate thermostable variants of mesophilic proteins. To gain insight into the mechanisms by which proteins become more stable, we use structural and dynamic analyses to compare two popular approaches, ancestral sequence reconstruction (ASR) and the consensus method, used to generate thermostable variants of Elongation Factor Thermo-unstable (EF-Tu). We present crystal structures of ancestral and consensus EF-Tus, accompanied by molecular dynamics simulations aimed at probing the strategies employed to enhance thermostability. All proteins adopt crystal structures similar to extant EF-Tus, revealing no difference in average structure between the methods. Molecular dynamics reveals that ASR-generated sequences retain dynamic properties similar to extant, thermostable EF-Tu from Thermus aquaticus, while consensus EF-Tu dynamics differ from evolution-based sequences. This work highlights the advantage of ASR for engineering thermostability while preserving natural motions in multidomain proteins.
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Structural and Dynamics Comparison of Thermostability in Ancient, Modern, and Consensus Elongation Factor Tus.,Okafor CD, Pathak MC, Fagan CE, Bauer NC, Cole MF, Gaucher EA, Ortlund EA Structure. 2018 Jan 2;26(1):118-129.e3. doi: 10.1016/j.str.2017.11.018. Epub 2017, Dec 21. PMID:29276038<ref>PMID:29276038</ref>
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==See Also==
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*[[Elongation factor 3D structures|Elongation factor 3D structures]]
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 5w75" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Ortlund, E A]]
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[[Category: Large Structures]]
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[[Category: Ancestral gene reconstruction]]
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[[Category: Thermotoga neapolitana DSM 4359]]
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[[Category: Asr]]
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[[Category: Ortlund EA]]
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[[Category: Ef-tu]]
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[[Category: Thermostability]]
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[[Category: Translation]]
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Current revision

Crystal Structure of Reconstructed Bacterial Elongation Factor Node 168

PDB ID 5w75

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