6rji
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==X-ray structure of the elongation factor P of S. aureus== | |
| + | <StructureSection load='6rji' size='340' side='right'caption='[[6rji]], [[Resolution|resolution]] 1.48Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[6rji]] is a 1 chain structure. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6RJI FirstGlance]. <br> | ||
| + | </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=6rji FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6rji OCA], [http://pdbe.org/6rji PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6rji RCSB], [http://www.ebi.ac.uk/pdbsum/6rji PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6rji ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [[http://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. | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == 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®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| - | [[Category: Gabdulkhakov, A | + | <div class="pdbe-citations 6rji" style="background-color:#fffaf0;"></div> |
| - | [[Category: Golubev, A | + | == References == |
| - | [[Category: Khusainov, I | + | <references/> |
| - | [[Category: | + | __TOC__ |
| - | [[Category: | + | </StructureSection> |
| - | + | [[Category: Large Structures]] | |
| - | [[Category: | + | [[Category: Fatkhullin, B F]] |
| + | [[Category: Gabdulkhakov, A G]] | ||
| + | [[Category: Golubev, A A]] | ||
| + | [[Category: Khusainov, I S]] | ||
| + | [[Category: Usachev, K S]] | ||
| + | [[Category: Validov, S Z]] | ||
| + | [[Category: Yusupov, M M]] | ||
[[Category: Yusupova, G]] | [[Category: Yusupova, G]] | ||
| + | [[Category: Ef-p]] | ||
| + | [[Category: Efp]] | ||
| + | [[Category: Elongation factor p]] | ||
| + | [[Category: Translation]] | ||
Revision as of 09:19, 1 April 2020
X-ray structure of the elongation factor P of S. aureus
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