View source for 6rji


==X-ray structure of the elongation factor P of S. aureus==
<StructureSection load='6rji' size='340' side='right'caption='[[6rji]], [[Resolution|resolution]] 1.48&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[6rji]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Staphylococcus_aureus_subsp._aureus_NCTC_8325 Staphylococcus aureus subsp. aureus NCTC 8325]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6RJI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6RJI FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.48&#8491;</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=6rji FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6rji OCA], [https://pdbe.org/6rji PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6rji RCSB], [https://www.ebi.ac.uk/pdbsum/6rji PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6rji ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/EFP_STAA8 EFP_STAA8] 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.
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== Publication Abstract from PubMed ==
Elongation factor P (EF-P) is a translation protein factor that plays an important role in specialized translation of consecutive proline amino acid motifs. EF-P is an essential protein for cell fitness in native environmental conditions. It regulates synthesis of proteins involved in bacterial motility, environmental adaptation and bacterial virulence, thus making EF-P a potential drug target. In the present study, we determined the solution and crystal structure of EF-P from the pathogenic bacteria Staphylococcus aureus at 1.48 A resolution. The structure can serve as a platform for structure-based drug design of novel antibiotics to combat the growing antibiotic resistance of S. aureus.

NMR and crystallographic structural studies of the Elongation factor P from Staphylococcus aureus.,Golubev A, Fatkhullin B, Gabdulkhakov A, Bikmullin A, Nurullina L, Garaeva N, Islamov D, Klochkova E, Klochkov V, Aganov A, Khusainov I, Validov S, Yusupova G, Yusupov M, Usachev K Eur Biophys J. 2020 Mar 9. pii: 10.1007/s00249-020-01428-x. doi:, 10.1007/s00249-020-01428-x. PMID:32152681<ref>PMID:32152681</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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<div class="pdbe-citations 6rji" style="background-color:#fffaf0;"></div>

==See Also==
*[[Elongation factor 3D structures|Elongation factor 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Staphylococcus aureus subsp. aureus NCTC 8325]]
[[Category: Fatkhullin BF]]
[[Category: Gabdulkhakov AG]]
[[Category: Golubev AA]]
[[Category: Khusainov IS]]
[[Category: Usachev KS]]
[[Category: Validov SZ]]
[[Category: Yusupov MM]]
[[Category: Yusupova G]]