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3vcy

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==Structure of MurA (UDP-N-acetylglucosamine enolpyruvyl transferase), from Vibrio fischeri in complex with substrate UDP-N-acetylglucosamine and the drug fosfomycin.==
==Structure of MurA (UDP-N-acetylglucosamine enolpyruvyl transferase), from Vibrio fischeri in complex with substrate UDP-N-acetylglucosamine and the drug fosfomycin.==
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<StructureSection load='3vcy' size='340' side='right' caption='[[3vcy]], [[Resolution|resolution]] 1.93&Aring;' scene=''>
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<StructureSection load='3vcy' size='340' side='right'caption='[[3vcy]], [[Resolution|resolution]] 1.93&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[3vcy]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Aliivibrio_fischeri Aliivibrio fischeri]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3VCY OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3VCY FirstGlance]. <br>
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<table><tr><td colspan='2'>[[3vcy]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Aliivibrio_fischeri_MJ11 Aliivibrio fischeri MJ11]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3VCY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3VCY FirstGlance]. <br>
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</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FFQ:[(1R)-1-HYDROXYPROPYL]PHOSPHONIC+ACID'>FFQ</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene>, <scene name='pdbligand=UD1:URIDINE-DIPHOSPHATE-N-ACETYLGLUCOSAMINE'>UD1</scene><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]] 1.925&#8491;</td></tr>
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<tr><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">murA, VFMJ11_0391 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=668 Aliivibrio fischeri])</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=FFQ:[(1R)-1-HYDROXYPROPYL]PHOSPHONIC+ACID'>FFQ</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene>, <scene name='pdbligand=UD1:URIDINE-DIPHOSPHATE-N-ACETYLGLUCOSAMINE'>UD1</scene></td></tr>
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<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/UDP-N-acetylglucosamine_1-carboxyvinyltransferase UDP-N-acetylglucosamine 1-carboxyvinyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.5.1.7 2.5.1.7] </span></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=3vcy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3vcy OCA], [https://pdbe.org/3vcy PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3vcy RCSB], [https://www.ebi.ac.uk/pdbsum/3vcy PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3vcy ProSAT]</span></td></tr>
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<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3vcy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3vcy OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3vcy RCSB], [http://www.ebi.ac.uk/pdbsum/3vcy PDBsum]</span></td></tr>
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</table>
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<table>
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== Function ==
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<div style="background-color:#fffaf0;">
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[https://www.uniprot.org/uniprot/MURA_ALIFM MURA_ALIFM] Cell wall formation. Adds enolpyruvyl to UDP-N-acetylglucosamine.[HAMAP-Rule:MF_00111]
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== Publication Abstract from PubMed ==
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The development of new antibiotics is necessitated by the rapid development of resistance to current therapies. UDP-N-acetylglucosamine enolpyruvyl transferase (MurA), which catalyzes the first committed step of bacterial peptidoglycan biosynthesis, is a prime candidate for therapeutic intervention. MurA is the target of the antibiotic fosfomycin, a natural product produced by Streptomyces. Despite possessing a high degree of sequence conservation with MurA enzymes from fosfomycin-susceptible organisms, recent microbiological studies suggest that MurA from Vibrio fischeri (VfiMurA) may confer fosfomycin resistance via a mechanism that is not yet understood. The crystal structure of VfiMurA in a ternary complex with the substrate UDP-N-acetylglucosamine (UNAG) and fosfomycin has been solved to a resolution of 1.93 A. Fosfomycin is known to inhibit MurA by covalently binding to a highly conserved cysteine in the active site of the enzyme. A comparison of the title structure with the structure of fosfomycin-susceptible Haemophilus influenzae MurA (PDB entry 2rl2) revealed strikingly similar conformations of the mobile substrate-binding loop and clear electron density for a fosfomycin-cysteine adduct. Based on these results, there are no distinguishing sequence/structural features in VfiMurA that would translate to a diminished sensitivity to fosfomycin. However, VfiMurA is a robust crystallizer and shares high sequence identity with many clinically relevant bacterial pathogens. Thus, it would serve as an ideal system for use in the structure-guided optimization of new antibacterial agents.
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Structure of MurA (UDP-N-acetylglucosamine enolpyruvyl transferase) from Vibrio fischeri in complex with substrate UDP-N-acetylglucosamine and the drug fosfomycin.,Bensen DC, Rodriguez S, Nix J, Cunningham ML, Tari LW Acta Crystallogr Sect F Struct Biol Cryst Commun. 2012 Apr 1;68(Pt 4):382-5. Epub, 2012 Mar 27. PMID:22505403<ref>PMID:22505403</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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==See Also==
==See Also==
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*[[Enoylpyruvate transferase|Enoylpyruvate transferase]]
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*[[Enoylpyruvate transferase 3D structures|Enoylpyruvate transferase 3D structures]]
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Aliivibrio fischeri]]
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[[Category: Aliivibrio fischeri MJ11]]
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[[Category: UDP-N-acetylglucosamine 1-carboxyvinyltransferase]]
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[[Category: Large Structures]]
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[[Category: Bensen, D C.]]
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[[Category: Bensen DC]]
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[[Category: Cunningham, M L.]]
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[[Category: Cunningham ML]]
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[[Category: Nix, J.]]
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[[Category: Nix J]]
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[[Category: Rodriguez, S.]]
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[[Category: Rodriguez S]]
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[[Category: Tari, L W.]]
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[[Category: Tari LW]]
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[[Category: Amino sugar and nucleotide sugar metabolism]]
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[[Category: Cytosol]]
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[[Category: Fosfomycin]]
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[[Category: Mura]]
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[[Category: Peptidoglycan]]
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[[Category: Peptidoglycan biosynthesis]]
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[[Category: Transferase-antibiotic complex]]
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Current revision

Structure of MurA (UDP-N-acetylglucosamine enolpyruvyl transferase), from Vibrio fischeri in complex with substrate UDP-N-acetylglucosamine and the drug fosfomycin.

PDB ID 3vcy

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