1naw

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[[Image:1naw.gif|left|200px]]
 
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==ENOLPYRUVYL TRANSFERASE==
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The line below this paragraph, containing "STRUCTURE_1naw", creates the "Structure Box" on the page.
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<StructureSection load='1naw' size='340' side='right'caption='[[1naw]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<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>
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or leave the SCENE parameter empty for the default display.
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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]] 2&#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=HAI:CYCLOHEXYLAMMONIUM+ION'>HAI</scene></td></tr>
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{{STRUCTURE_1naw| PDB=1naw | SCENE= }}
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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=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>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/MURA_ENTCC MURA_ENTCC] Cell wall formation. Adds enolpyruvyl to UDP-N-acetylglucosamine. Target for the antibiotic phosphomycin.
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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/na/1naw_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=1naw ConSurf].
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<div style="clear:both"></div>
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'''ENOLPYRUVYL TRANSFERASE'''
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==See Also==
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*[[Enoylpyruvate transferase 3D structures|Enoylpyruvate transferase 3D structures]]
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__TOC__
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==Overview==
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</StructureSection>
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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.
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==About this Structure==
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1NAW is a [[Single protein]] structure of sequence from [http://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].
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==Reference==
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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://www.ncbi.nlm.nih.gov/pubmed/8805592 8805592]
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[[Category: Enterobacter cloacae]]
[[Category: Enterobacter cloacae]]
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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: Amrhein N]]
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[[Category: Amrhein, N.]]
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[[Category: Eschenburg S]]
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[[Category: Eschenburg, S.]]
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[[Category: Krekel F]]
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[[Category: Krekel, F.]]
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[[Category: Mandelkow E]]
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[[Category: Mandelkow, E.]]
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[[Category: Perrakis A]]
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[[Category: Perrakis, A.]]
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[[Category: Sack S]]
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[[Category: Sack, S.]]
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[[Category: Schoenbrunn E]]
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[[Category: Schoenbrunn, E.]]
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[[Category: Domain movement]]
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[[Category: Folding]]
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[[Category: Hinge]]
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[[Category: Peptidoglycan biosynthesis]]
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[[Category: Sequence motif]]
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[[Category: Transferase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 02:18:32 2008''
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Current revision

ENOLPYRUVYL TRANSFERASE

PDB ID 1naw

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