5nv8

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m (Protected "5nv8" [edit=sysop:move=sysop])
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'''Unreleased structure'''
 
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The entry 5nv8 is ON HOLD
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==Structural basis for EarP-mediated arginine glycosylation of translation elongation factor EF-P==
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<StructureSection load='5nv8' size='340' side='right' caption='[[5nv8]], [[Resolution|resolution]] 2.29&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[5nv8]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5NV8 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5NV8 FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=TRH:2-DEOXY-THYMIDINE-BETA-L-RHAMNOSE'>TRH</scene></td></tr>
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<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=5nv8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5nv8 OCA], [http://pdbe.org/5nv8 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5nv8 RCSB], [http://www.ebi.ac.uk/pdbsum/5nv8 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5nv8 ProSAT]</span></td></tr>
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</table>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Glycosylation is a universal strategy to posttranslationally modify proteins. The recently discovered arginine rhamnosylation activates the polyproline-specific bacterial translation elongation factor EF-P. EF-P is rhamnosylated on arginine 32 by the glycosyltransferase EarP. However, the enzymatic mechanism remains elusive. In the present study, we solved the crystal structure of EarP from Pseudomonas putida The enzyme is composed of two opposing domains with Rossmann folds, thus constituting a B pattern-type glycosyltransferase (GT-B). While dTDP-beta-l-rhamnose is located within a highly conserved pocket of the C-domain, EarP recognizes the KOW-like N-domain of EF-P. Based on our data, we propose a structural model for arginine glycosylation by EarP. As EarP is essential for pathogenicity in P. aeruginosa, our study provides the basis for targeted inhibitor design.IMPORTANCE The structural and biochemical characterization of the EF-P-specific rhamnosyltransferase EarP not only provides the first molecular insights into arginine glycosylation but also lays the basis for targeted-inhibitor design against Pseudomonas aeruginosa infection.
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Authors:
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Structural Basis for EarP-Mediated Arginine Glycosylation of Translation Elongation Factor EF-P.,Krafczyk R, Macosek J, Jagtap PKA, Gast D, Wunder S, Mitra P, Jha AK, Rohr J, Hoffmann-Roder A, Jung K, Hennig J, Lassak J MBio. 2017 Sep 26;8(5). pii: e01412-17. doi: 10.1128/mBio.01412-17. PMID:28951478<ref>PMID:28951478</ref>
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Description:
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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[[Category: Unreleased Structures]]
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</div>
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<div class="pdbe-citations 5nv8" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Jagtap, P K.A]]
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[[Category: Krafczyk, R]]
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[[Category: Macosek, J]]
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[[Category: Glycosyltransferase]]
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[[Category: Transferase]]

Revision as of 06:45, 11 October 2017

Structural basis for EarP-mediated arginine glycosylation of translation elongation factor EF-P

5nv8, resolution 2.29Å

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