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| <StructureSection load='7cdw' size='340' side='right'caption='[[7cdw]], [[Resolution|resolution]] 3.00Å' scene=''> | | <StructureSection load='7cdw' size='340' side='right'caption='[[7cdw]], [[Resolution|resolution]] 3.00Å' scene=''> |
| == Structural highlights == | | == Structural highlights == |
| <table><tr><td colspan='2'>[[7cdw]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7CDW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7CDW FirstGlance]. <br> | | <table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7CDW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7CDW FirstGlance]. <br> |
| </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GDP:GUANOSINE-5-DIPHOSPHATE'>GDP</scene></td></tr> | | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3Å</td></tr> |
| <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> | | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GDP:GUANOSINE-5-DIPHOSPHATE'>GDP</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></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=7cdw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7cdw OCA], [https://pdbe.org/7cdw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7cdw RCSB], [https://www.ebi.ac.uk/pdbsum/7cdw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7cdw ProSAT]</span></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=7cdw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7cdw OCA], [https://pdbe.org/7cdw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7cdw RCSB], [https://www.ebi.ac.uk/pdbsum/7cdw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7cdw ProSAT]</span></td></tr> |
| </table> | | </table> |
| == Function ==
| |
| [[https://www.uniprot.org/uniprot/EFG_MYCTU EFG_MYCTU]] Catalyzes the GTP-dependent ribosomal translocation step during translation elongation. During this step, the ribosome changes from the pre-translocational (PRE) to the post-translocational (POST) state as the newly formed A-site-bound peptidyl-tRNA and P-site-bound deacylated tRNA move to the P and E sites, respectively. Catalyzes the coordinated movement of the two tRNA molecules, the mRNA and conformational changes in the ribosome (By similarity).
| |
| <div style="background-color:#fffaf0;">
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| == Publication Abstract from PubMed ==
| |
| Mycobacterium tuberculosis (Mtb) caused an estimated 10 million cases of tuberculosis and 1.2 million deaths in 2019 globally. The increasing emergence of multidrug-resistant and extensively drug-resistant Mtb is becoming a public health threat worldwide and makes the identification of anti-Mtb drug targets urgent. Elongation factor G (EF-G) is involved in tRNA translocation on ribosomes during protein translation. Therefore, EF-G is a major focus of structural analysis and a valuable drug target of antibiotics. However, the crystal structure of Mtb EF-G1 is not yet available, and this has limited the design of inhibitors. Here, we report the crystal structure of Mtb EF-G1 in complex with GDP. The unique crystal form of the Mtb EF-G1-GDP complex provides an excellent platform for fragment-based screening using a crystallographic approach. Our findings provide a structure-based explanation for GDP recognition, and facilitate the identification of EF-G1 inhibitors with potential interest in the context of drug discovery.
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| Crystal Structure of Mycobacterium tuberculosis Elongation Factor G1.,Gao X, Yu X, Zhu K, Qin B, Wang W, Han P, Aleksandra Wojdyla J, Wang M, Cui S Front Mol Biosci. 2021 Sep 3;8:667638. doi: 10.3389/fmolb.2021.667638., eCollection 2021. PMID:34540889<ref>PMID:34540889</ref>
| | ==See Also== |
| | | *[[Elongation factor 3D structures|Elongation factor 3D structures]] |
| From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
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| </div>
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| <div class="pdbe-citations 7cdw" style="background-color:#fffaf0;"></div>
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| == References == | |
| <references/>
| |
| __TOC__ | | __TOC__ |
| </StructureSection> | | </StructureSection> |
| [[Category: Large Structures]] | | [[Category: Large Structures]] |
| [[Category: Cui, S]] | | [[Category: Cui S]] |
| [[Category: Gao, X]] | | [[Category: Gao X]] |
| [[Category: Antituberculosis drug]]
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| [[Category: Crystal structure]]
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| [[Category: Gtpase]]
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| [[Category: Hydrolase]]
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| [[Category: Ribosome-bound ef-g]]
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