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New page: left|200px<br /><applet load="1naw" size="450" color="white" frame="true" align="right" spinBox="true" caption="1naw, resolution 2.0Å" /> '''ENOLPYRUVYL TRANSFERA...
 
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[[Image:1naw.gif|left|200px]]<br /><applet load="1naw" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1naw, resolution 2.0&Aring;" />
'''ENOLPYRUVYL TRANSFERASE'''<br />


==Overview==
==ENOLPYRUVYL TRANSFERASE==
BACKGROUND. The ever increasing number of antibiotic resistant bacteria, has fuelled interest in the development of new antibiotics and other, antibacterial agents. The major structural element of the bacterial cell, wall is the heteropolymer peptidoglycan and the enzymes of peptidoglycan, biosynthesis are potential targets for antibacterial agents. One such, enzyme is UDP-N-acetylglucosamine enolpyruvyltransferase (EPT) which, catalyzes the first committed step in peptidoglycan biosynthesis: the, transfer of the enolpyruvyl moiety of phosphoenolpyruvate (PEP) to the, 3-hydroxyl of UDP-N-acetylglucosamine (UDPGlcNAc). EPT is of potential, pharmaceutical interest because it is inhibited by the broad spectrum, antibiotic fosfomycin. RESULTS. The crystal structure of substrate-free, EPT has been determined at 2.0 A resolution. The structure reveals a, two-domain protein with an unusual fold (inside out alpha/beta barrel), which is built up from the sixfold repetition of one folding unit. The, only repetitive element in the amino acid sequence is a short motif, Leu-X3-Gly(Ala), which is responsible for the formation of hydrogen-bond, interactions between the folding units. An enzyme which catalyzes a, similar reaction to EPT, 5-enolpyruvylshikimate-3-phosphate synthase, (EPSPS), has a very similar structure despite an amino acid sequence, identity of only 25%. To date, only these two enzymes appear to display, this characteristic fold. CONCLUSIONS. The present structure reflects the, open conformation of the enzyme which is probably stabilized through two, residues, a lysine and an arginine, located in the cleft between the, domains. Binding of the negatively charged UDPGlcNAc to these residues, could neutralize the repulsive force between the two domains, thereby, allowing the movement of a catalytically active cysteine residue towards, the cleft.
<StructureSection load='1naw' size='340' side='right'caption='[[1naw]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1naw]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Enterobacter_cloacae Enterobacter cloacae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NAW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1NAW 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]] 2&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=HAI:CYCLOHEXYLAMMONIUM+ION'>HAI</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=1naw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1naw OCA], [https://pdbe.org/1naw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1naw RCSB], [https://www.ebi.ac.uk/pdbsum/1naw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1naw ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/MURA_ENTCC MURA_ENTCC] Cell wall formation. Adds enolpyruvyl to UDP-N-acetylglucosamine. Target for the antibiotic phosphomycin.
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/na/1naw_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</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=1naw ConSurf].
<div style="clear:both"></div>


==About this Structure==
==See Also==
1NAW is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Enterobacter_cloacae Enterobacter cloacae] with HAI as [http://en.wikipedia.org/wiki/ligand ligand]. 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=1NAW OCA].
*[[Enoylpyruvate transferase 3D structures|Enoylpyruvate transferase 3D structures]]
 
__TOC__
==Reference==
</StructureSection>
Crystal structure of UDP-N-acetylglucosamine enolpyruvyltransferase, the target of the antibiotic fosfomycin., Schonbrunn E, Sack S, Eschenburg S, Perrakis A, Krekel F, Amrhein N, Mandelkow E, Structure. 1996 Sep 15;4(9):1065-75. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=8805592 8805592]
[[Category: Enterobacter cloacae]]
[[Category: Enterobacter cloacae]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: UDP-N-acetylglucosamine 1-carboxyvinyltransferase]]
[[Category: Amrhein N]]
[[Category: Amrhein, N.]]
[[Category: Eschenburg S]]
[[Category: Eschenburg, S.]]
[[Category: Krekel F]]
[[Category: Krekel, F.]]
[[Category: Mandelkow E]]
[[Category: Mandelkow, E.]]
[[Category: Perrakis A]]
[[Category: Perrakis, A.]]
[[Category: Sack S]]
[[Category: Sack, S.]]
[[Category: Schoenbrunn E]]
[[Category: Schoenbrunn, E.]]
[[Category: HAI]]
[[Category: domain movement]]
[[Category: folding]]
[[Category: hinge]]
[[Category: peptidoglycan biosynthesis]]
[[Category: sequence motif]]
[[Category: transferase]]
 
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Retrieved from "https://proteopedia.org/1naw"