6rk3: Difference between revisions
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<StructureSection load='6rk3' size='340' side='right'caption='[[6rk3]], [[NMR_Ensembles_of_Models | 10 NMR models]]' scene=''> | <StructureSection load='6rk3' size='340' side='right'caption='[[6rk3]], [[NMR_Ensembles_of_Models | 10 NMR models]]' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[6rk3]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6RK3 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6RK3 FirstGlance]. <br> | <table><tr><td colspan='2'>[[6rk3]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"micrococcus_aureus"_(rosenbach_1884)_zopf_1885 "micrococcus aureus" (rosenbach 1884) zopf 1885]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6RK3 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6RK3 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=6rk3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6rk3 OCA], [http://pdbe.org/6rk3 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6rk3 RCSB], [http://www.ebi.ac.uk/pdbsum/6rk3 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6rk3 ProSAT]</span></td></tr> | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">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 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1280 "Micrococcus aureus" (Rosenbach 1884) Zopf 1885])</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=6rk3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6rk3 OCA], [http://pdbe.org/6rk3 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6rk3 RCSB], [http://www.ebi.ac.uk/pdbsum/6rk3 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6rk3 ProSAT]</span></td></tr> | |||
</table> | </table> | ||
== Function == | == Function == | ||
[[http://www.uniprot.org/uniprot/W8U5N1_STAAU 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] | [[http://www.uniprot.org/uniprot/W8U5N1_STAAU 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] | ||
<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> | |||
</div> | |||
<div class="pdbe-citations 6rk3" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
Revision as of 13:26, 18 March 2020
Solution structure of the ribosome Elongation Factor P (EF-P) from Staphylococcus aureusSolution structure of the ribosome Elongation Factor P (EF-P) from Staphylococcus aureus
Structural highlights
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 PubMedElongation 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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