4y7u

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(New page: '''Unreleased structure''' The entry 4y7u is ON HOLD Authors: Renner-Schneck, M.G., Stehle, T. Description: Structural analysis of MurU Category: Unreleased Structures [[Category: ...)
Current revision (11:30, 9 May 2024) (edit) (undo)
 
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'''Unreleased structure'''
 
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The entry 4y7u is ON HOLD
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==Structural analysis of MurU==
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<StructureSection load='4y7u' size='340' side='right'caption='[[4y7u]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[4y7u]] 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=4Y7U OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4Y7U FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.7&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=2KH:5-O-[(S)-HYDROXY{[(S)-HYDROXY(PHOSPHONOOXY)PHOSPHORYL]AMINO}PHOSPHORYL]URIDINE'>2KH</scene>, <scene name='pdbligand=491:2-(ACETYLAMINO)-3-O-[(1R)-1-CARBOXYETHYL]-2-DEOXY-1-O-PHOSPHONO-ALPHA-D-GLUCOPYRANOSE'>491</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4y7u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4y7u OCA], [https://pdbe.org/4y7u PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4y7u RCSB], [https://www.ebi.ac.uk/pdbsum/4y7u PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4y7u ProSAT]</span></td></tr>
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</table>
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== Function ==
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[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>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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Authors: Renner-Schneck, M.G., Stehle, T.
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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>
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Description: Structural analysis of MurU
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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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[[Category: Stehle, T]]
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<div class="pdbe-citations 4y7u" style="background-color:#fffaf0;"></div>
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[[Category: Renner-Schneck, M.G]]
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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: Large Structures]]
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[[Category: Pseudomonas putida BIRD-1]]
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[[Category: Renner-Schneck MG]]
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[[Category: Stehle T]]

Current revision

Structural analysis of MurU

PDB ID 4y7u

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