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6rk3

From Proteopedia

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

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^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ 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. NMR and crystallographic structural studies of the Elongation factor P from Staphylococcus aureus. Eur Biophys J. 2020 Mar 9. pii: 10.1007/s00249-020-01428-x. doi:, 10.1007/s00249-020-01428-x. PMID:32152681 doi:http://dx.doi.org/10.1007/s00249-020-01428-x

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 See Also
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/6rk3"

@@ Line 3: / Line 3: @@
 <StructureSection load='6rk3' size='340' side='right'caption='[[6rk3]], [[NMR_Ensembles_of_Models | 10 NMR models]]' scene=''>
 == Structural highlights ==
-<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://proteopedia.org/fgij/fg.htm?mol=6RK3 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[6rk3]] is a 1 chain structure with sequence from [https://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 [https://proteopedia.org/fgij/fg.htm?mol=6RK3 FirstGlance]. <br>
-</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>
+</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 ([https://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://proteopedia.org/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>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=6rk3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6rk3 OCA], [https://pdbe.org/6rk3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6rk3 RCSB], [https://www.ebi.ac.uk/pdbsum/6rk3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6rk3 ProSAT]</span></td></tr>
 </table>
 == 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]
+[[https://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 ==
@@ Line 18: / Line 18: @@
 </div>
 <div class="pdbe-citations 6rk3" style="background-color:#fffaf0;"></div>
+==See Also==
+*[[Elongation factor 3D structures|Elongation factor 3D structures]]
 == References ==
 <references/>

6rk3

From Proteopedia

Current revision

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

Structural highlights

Function

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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