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| | <StructureSection load='6s8z' size='340' side='right'caption='[[6s8z]], [[Resolution|resolution]] 2.20Å' scene=''> | | <StructureSection load='6s8z' size='340' side='right'caption='[[6s8z]], [[Resolution|resolution]] 2.20Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[6s8z]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"micrococcus_glutamicus"_kinoshita_et_al._1958 "micrococcus glutamicus" kinoshita et al. 1958]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6S8Z OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6S8Z FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6s8z]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Corynebacterium_glutamicum Corynebacterium glutamicum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6S8Z OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6S8Z FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</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]] 2.2Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">efp, CS176_1554 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1718 "Micrococcus glutamicus" Kinoshita et al. 1958])</td></tr>
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=6s8z FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6s8z OCA], [http://pdbe.org/6s8z PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6s8z RCSB], [http://www.ebi.ac.uk/pdbsum/6s8z PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6s8z 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=6s8z FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6s8z OCA], [https://pdbe.org/6s8z PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6s8z RCSB], [https://www.ebi.ac.uk/pdbsum/6s8z PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6s8z ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/A0A1B4WLR4_CORGT A0A1B4WLR4_CORGT]] Involved in peptide bond synthesis. Stimulates efficient translation and peptide-bond synthesis on native or reconstituted 70S ribosomes in vitro. Probably functions indirectly by altering the affinity of the ribosome for aminoacyl-tRNA, thus increasing their reactivity as acceptors for peptidyl transferase.[HAMAP-Rule:MF_00141] | + | [https://www.uniprot.org/uniprot/EFP_CORGL EFP_CORGL] Involved in peptide bond synthesis. Stimulates efficient translation and peptide-bond synthesis on native or reconstituted 70S ribosomes in vitro. Probably functions indirectly by altering the affinity of the ribosome for aminoacyl-tRNA, thus increasing their reactivity as acceptors for peptidyl transferase (By similarity). |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | </div> | | </div> |
| | <div class="pdbe-citations 6s8z" style="background-color:#fffaf0;"></div> | | <div class="pdbe-citations 6s8z" style="background-color:#fffaf0;"></div> |
| | + | |
| | + | ==See Also== |
| | + | *[[Elongation factor 3D structures|Elongation factor 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Micrococcus glutamicus kinoshita et al. 1958]] | + | [[Category: Corynebacterium glutamicum]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Scheidler, C M]] | + | [[Category: Scheidler CM]] |
| - | [[Category: Schneider, S]] | + | [[Category: Schneider S]] |
| - | [[Category: Elongation factor p]]
| + | |
| - | [[Category: Translation]]
| + | |
| Structural highlights
Function
EFP_CORGL Involved in peptide bond synthesis. Stimulates efficient translation and peptide-bond synthesis on native or reconstituted 70S ribosomes in vitro. Probably functions indirectly by altering the affinity of the ribosome for aminoacyl-tRNA, thus increasing their reactivity as acceptors for peptidyl transferase (By similarity).
Publication Abstract from PubMed
Translation of consecutive proline motifs causes ribosome stalling and requires rescue via the action of a specific translation elongation factor, EF-P in bacteria and archaeal/eukaryotic a/eIF5A. In Eukarya, Archaea, and all bacteria investigated so far, the functionality of this translation elongation factor depends on specific and rather unusual post-translational modifications. The phylum Actinobacteria, which includes the genera Corynebacterium, Mycobacterium, and Streptomyces, is of both medical and economic significance. Here, we report that EF-P is required in these bacteria in particular for the translation of proteins involved in amino acid and secondary metabolite production. Notably, EF-P of Actinobacteria species does not need any post-translational modification for activation. While the function and overall 3D structure of this EF-P type is conserved, the loop containing the conserved lysine is flanked by two essential prolines that rigidify it. Actinobacteria's EF-P represents a unique subfamily that works without any modification.
Structure and Function of an Elongation Factor P Subfamily in Actinobacteria.,Pinheiro B, Scheidler CM, Kielkowski P, Schmid M, Forne I, Ye S, Reiling N, Takano E, Imhof A, Sieber SA, Schneider S, Jung K Cell Rep. 2020 Mar 31;30(13):4332-4342.e5. doi: 10.1016/j.celrep.2020.03.009. PMID:32234471[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Pinheiro B, Scheidler CM, Kielkowski P, Schmid M, Forne I, Ye S, Reiling N, Takano E, Imhof A, Sieber SA, Schneider S, Jung K. Structure and Function of an Elongation Factor P Subfamily in Actinobacteria. Cell Rep. 2020 Mar 31;30(13):4332-4342.e5. doi: 10.1016/j.celrep.2020.03.009. PMID:32234471 doi:http://dx.doi.org/10.1016/j.celrep.2020.03.009
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