2mzw: Difference between revisions

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==Staphylococcus aureus FusB:EF-GC3 complex==
==Staphylococcus aureus FusB:EF-GC3 complex==
<StructureSection load='2mzw' size='340' side='right' caption='[[2mzw]], [[NMR_Ensembles_of_Models | 1 NMR models]]' scene=''>
<StructureSection load='2mzw' size='340' side='right'caption='[[2mzw]], [[NMR_Ensembles_of_Models | 1 NMR models]]' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[2mzw]] is a 2 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=2MZW OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2MZW FirstGlance]. <br>
<table><tr><td colspan='2'>[[2mzw]] is a 2 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=2MZW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2MZW FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2xex|2xex]], [[4adn|4adn]]</td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2xex|2xex]], [[4adn|4adn]]</div></td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">CH51_02860, CH52_03020, DA92_03395, DP18_1097, EX97_02750, fusA, SAU060112_10722, SAXN108_0601, X998_0588 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1280 "Micrococcus aureus" (Rosenbach 1884) Zopf 1885]), far1, fusB ([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='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">CH51_02860, CH52_03020, DA92_03395, DP18_1097, EX97_02750, fusA, SAU060112_10722, SAXN108_0601, X998_0588 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1280 "Micrococcus aureus" (Rosenbach 1884) Zopf 1885]), far1, fusB ([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://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2mzw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2mzw OCA], [http://pdbe.org/2mzw PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2mzw RCSB], [http://www.ebi.ac.uk/pdbsum/2mzw PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2mzw 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=2mzw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2mzw OCA], [https://pdbe.org/2mzw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2mzw RCSB], [https://www.ebi.ac.uk/pdbsum/2mzw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2mzw ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/W8UT26_STAAU W8UT26_STAAU]] Catalyzes the GTP-dependent ribosomal translocation step during translation elongation. During this step, the ribosome changes from the pre-translocational (PRE) to the post-translocational (POST) state as the newly formed A-site-bound peptidyl-tRNA and P-site-bound deacylated tRNA move to the P and E sites, respectively. Catalyzes the coordinated movement of the two tRNA molecules, the mRNA and conformational changes in the ribosome.[HAMAP-Rule:MF_00054]  
[[https://www.uniprot.org/uniprot/W8UT26_STAAU W8UT26_STAAU]] Catalyzes the GTP-dependent ribosomal translocation step during translation elongation. During this step, the ribosome changes from the pre-translocational (PRE) to the post-translocational (POST) state as the newly formed A-site-bound peptidyl-tRNA and P-site-bound deacylated tRNA move to the P and E sites, respectively. Catalyzes the coordinated movement of the two tRNA molecules, the mRNA and conformational changes in the ribosome.[HAMAP-Rule:MF_00054]  
<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Kalverda, A P]]
[[Category: Kalverda, A P]]
[[Category: Neill, A O]]
[[Category: Neill, A O]]

Revision as of 18:24, 2 June 2021

Staphylococcus aureus FusB:EF-GC3 complexStaphylococcus aureus FusB:EF-GC3 complex

Structural highlights

2mzw is a 2 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.
Ligands:
Gene:CH51_02860, CH52_03020, DA92_03395, DP18_1097, EX97_02750, fusA, SAU060112_10722, SAXN108_0601, X998_0588 ("Micrococcus aureus" (Rosenbach 1884) Zopf 1885), far1, fusB ("Micrococcus aureus" (Rosenbach 1884) Zopf 1885)
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[W8UT26_STAAU] Catalyzes the GTP-dependent ribosomal translocation step during translation elongation. During this step, the ribosome changes from the pre-translocational (PRE) to the post-translocational (POST) state as the newly formed A-site-bound peptidyl-tRNA and P-site-bound deacylated tRNA move to the P and E sites, respectively. Catalyzes the coordinated movement of the two tRNA molecules, the mRNA and conformational changes in the ribosome.[HAMAP-Rule:MF_00054]

Publication Abstract from PubMed

Antibiotic resistance in clinically important bacteria can be mediated by proteins that physically associate with the drug target and act to protect it from the inhibitory effects of an antibiotic. We present here the first detailed structural characterization of such a target protection mechanism mediated through a protein-protein interaction, revealing the architecture of the complex formed between the FusB fusidic acid resistance protein and the drug target (EF-G) it acts to protect. Binding of FusB to EF-G induces conformational and dynamic changes in the latter, shedding light on the molecular mechanism of fusidic acid resistance.

A target-protection mechanism of antibiotic resistance at atomic resolution: insights into FusB-type fusidic acid resistance.,Tomlinson JH, Thompson GS, Kalverda AP, Zhuravleva A, O'Neill AJ Sci Rep. 2016 Jan 19;6:19524. doi: 10.1038/srep19524. PMID:26781961[1]

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

References

  1. Tomlinson JH, Thompson GS, Kalverda AP, Zhuravleva A, O'Neill AJ. A target-protection mechanism of antibiotic resistance at atomic resolution: insights into FusB-type fusidic acid resistance. Sci Rep. 2016 Jan 19;6:19524. doi: 10.1038/srep19524. PMID:26781961 doi:http://dx.doi.org/10.1038/srep19524
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