4y7t
From Proteopedia
(Difference between revisions)
(New page: '''Unreleased structure''' The entry 4y7t is ON HOLD Authors: Renner-Schneck, M.G., Stehle, T. Description: Structural analysis of MurU Category: Unreleased Structures [[Category: ...) |
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| - | '''Unreleased structure''' | ||
| - | + | ==Structural analysis of MurU== | |
| + | <StructureSection load='4y7t' size='340' side='right'caption='[[4y7t]], [[Resolution|resolution]] 1.80Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[4y7t]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudomonas_putida_BIRD-1 Pseudomonas putida BIRD-1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4Y7T OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4Y7T FirstGlance]. <br> | ||
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.8Å</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></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=4y7t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4y7t OCA], [https://pdbe.org/4y7t PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4y7t RCSB], [https://www.ebi.ac.uk/pdbsum/4y7t PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4y7t ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/MURU_PSEPK MURU_PSEPK] Catalyzes the formation of UDP-N-acetylmuramate (UDP-MurNAc), a crucial precursor of the bacterial peptidoglycan cell wall, from UTP and MurNAc-alpha-1P (PubMed:23831760, PubMed:25767118). Is involved in peptidoglycan recycling as part of a cell wall recycling pathway that bypasses de novo biosynthesis of the peptidoglycan precursor UDP-MurNAc (PubMed:23831760). Plays a role in intrinsic resistance to fosfomycin, which targets the de novo synthesis of UDP-MurNAc (PubMed:23831760). Is not able to use GlcNAc-alpha-1P and GalNAc-alpha-1P as substrates (PubMed:23831760). Cannot accept other nucleotide triphosphates (ATP, CTP, TTP, or GTP) than UTP (PubMed:25767118).<ref>PMID:23831760</ref> <ref>PMID:25767118</ref> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | The N-acetylmuramic acid alpha-1-phosphate (MurNAc-alpha1P) uridylyltransferase MurU catalyzes the synthesis of uridine diphosphate (UDP)-MurNAc, a crucial precursor of the bacterial peptidoglycan cell wall. MurU is part of a recently identified cell wall recycling pathway in Gram-negative bacteria that bypasses the general de-novo biosynthesis of UDP-MurNAc and contributes to high intrinsic resistance to the antibiotic fosfomycin, which targets UDP-MurNAc de novo biosynthesis. To provide insights into substrate binding and specificity, we solved crystal structures of MurU of Pseudomonas putida in native and ligand-bound states at high resolution. With the help of these structures, critical enzyme- substrate interactions were identified that enable tight binding of MurNAc-alpha1P to the active site of MurU. The MurU structures define a "minimal domain" required for general nucleotidyltransferase activity. They furthermore provide a structural basis for the chemical design of inhibitors of MurU, which could serve as novel drugs in combination therapy against multi-resistant Gram-negative pathogens. | ||
| - | + | Crystal structure of the N-acetylmuramic acid alpha-1-phosphate (MurNAc-alpha1P) uridylytransferase MurU, a minimal sugar-nucleotidyltransferase and potential drug target enzyme in Gram-negative pathogens.,Renner-Schneck M, Hinderberger I, Gisin J, Exner T, Mayer C, Stehle T J Biol Chem. 2015 Mar 12. pii: jbc.M114.620989. PMID:25767118<ref>PMID:25767118</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| - | [[Category: | + | <div class="pdbe-citations 4y7t" style="background-color:#fffaf0;"></div> |
| - | [[Category: Renner-Schneck | + | == References == |
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Pseudomonas putida BIRD-1]] | ||
| + | [[Category: Renner-Schneck MG]] | ||
| + | [[Category: Stehle T]] | ||
Current revision
Structural analysis of MurU
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