6rk3 | pdb_00006rk3

Solution structure of the ribosome Elongation Factor P (EF-P) from Staphylococcus aureus

spinqualitylabelsall models 6rk3, 10 NMR models Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6rk3 is a 1 chain structure with sequence from "micrococcus_aureus"_(rosenbach_1884)_zopf_1885 "micrococcus aureus" (rosenbach 1884) zopf 1885. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance. Gene: efp, efp_1, BN1321_260166, BTN44_04530, CSC83_09570, CSC87_09360, CV021_16705, EP54_01240, EQ90_12570, ERS072840_00894, HMPREF3211_01680, M1K003_1282, NCTC10654_01594, NCTC13131_01960, NCTC13196_02506, NCTC6133_02039, NCTC7878_01463, RK64_08215, SAMEA1466939_00955, SAMEA1708674_01996 ("Micrococcus aureus" (Rosenbach 1884) Zopf 1885) Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [W8U5N1_STAAU] 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] 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Elongation factor 3D structures

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