1uae

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(New page: 200px<br /><applet load="1uae" size="450" color="white" frame="true" align="right" spinBox="true" caption="1uae, resolution 1.8&Aring;" /> '''STRUCTURE OF UDP-N-AC...)
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[[Image:1uae.jpg|left|200px]]<br /><applet load="1uae" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1uae, resolution 1.8&Aring;" />
 
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'''STRUCTURE OF UDP-N-ACETYLGLUCOSAMINE ENOLPYRUVYL TRANSFERASE'''<br />
 
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==Overview==
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==STRUCTURE OF UDP-N-ACETYLGLUCOSAMINE ENOLPYRUVYL TRANSFERASE==
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BACKGROUND: UDP-N-acetylglucosamine enolpyruvyl transferase (MurA), catalyses the first committed step of bacterial cell wall biosynthesis and, is a target for the antibiotic fosfomycin. The only other known, enolpyruvyl transferase is 5-enolpyruvylshikimate-3-phosphate (EPSP), synthase, an enzyme involved in the shikimic acid pathway and the target, for the herbicide glyphosate. Inhibitors of enolpyruvyl transferases are, of biotechnological interest as MurA and EPSP synthase are found, exclusively in plants and microbes. RESULTS: The crystal structure of, Escherichia coli MurA complexed with UDP-N-acetylglucosamine (UDP-GlcNAc), and fosfomycin has been determined at 1.8 A resolution. The structure, consists of two domains with the active site located between them. The, domains have a very similar secondary structure, and the overall protein, architecture is similar to that of EPSP synthase. The fosfomycin molecule, is covalently bound to the cysteine residue Cys115, whereas UDP-GlcNAc, makes several hydrogen-bonding interactions with residues from both, domains. CONCLUSIONS: The present structure reveals the mode of binding of, the natural substrate UDP-GlcNAc and of the drug fosfomycin, and provides, information on the residues involved in catalysis. These results should, aid the design of inhibitors which would interfere with enzyme-catalyzed, reactions in the early stage of the bacterial cell wall biosynthesis., Furthermore, the crystal structure of MurA provides a model for predicting, active-site residues in EPSP synthase that may be involved in catalysis, and substrate binding.
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<StructureSection load='1uae' size='340' side='right'caption='[[1uae]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1uae]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1UAE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1UAE 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]] 1.8&#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=FFQ:[(1R)-1-HYDROXYPROPYL]PHOSPHONIC+ACID'>FFQ</scene>, <scene name='pdbligand=UD1:URIDINE-DIPHOSPHATE-N-ACETYLGLUCOSAMINE'>UD1</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=1uae FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1uae OCA], [https://pdbe.org/1uae PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1uae RCSB], [https://www.ebi.ac.uk/pdbsum/1uae PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1uae ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/MURA_ECOLI MURA_ECOLI] Cell wall formation. Adds enolpyruvyl to UDP-N-acetylglucosamine. Target for the antibiotic phosphomycin.[HAMAP-Rule:MF_00111]
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ua/1uae_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1uae ConSurf].
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<div style="clear:both"></div>
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==About this Structure==
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==See Also==
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1UAE is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with UD1 and FCN as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [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] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1UAE OCA].
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*[[Enoylpyruvate transferase 3D structures|Enoylpyruvate transferase 3D structures]]
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__TOC__
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==Reference==
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</StructureSection>
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Structure of UDP-N-acetylglucosamine enolpyruvyl transferase, an enzyme essential for the synthesis of bacterial peptidoglycan, complexed with substrate UDP-N-acetylglucosamine and the drug fosfomycin., Skarzynski T, Mistry A, Wonacott A, Hutchinson SE, Kelly VA, Duncan K, Structure. 1996 Dec 15;4(12):1465-74. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=8994972 8994972]
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[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: UDP-N-acetylglucosamine 1-carboxyvinyltransferase]]
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[[Category: Skarzynski T]]
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[[Category: Skarzynski, T.]]
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[[Category: FCN]]
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[[Category: UD1]]
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[[Category: fosfomycin]]
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[[Category: peptidoglycan]]
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[[Category: transferase]]
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[[Category: udp-n-acetylglucosamine]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 03:57:42 2007''
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STRUCTURE OF UDP-N-ACETYLGLUCOSAMINE ENOLPYRUVYL TRANSFERASE

PDB ID 1uae

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