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1fwy

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(New page: 200px<br /><applet load="1fwy" size="450" color="white" frame="true" align="right" spinBox="true" caption="1fwy, resolution 2.3&Aring;" /> '''CRYSTAL STRUCTURE OF ...)
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[[Image:1fwy.jpg|left|200px]]<br /><applet load="1fwy" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1fwy, resolution 2.3&Aring;" />
 
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'''CRYSTAL STRUCTURE OF N-ACETYLGLUCOSAMINE 1-PHOSPHATE URIDYLTRANSFERASE BOUND TO UDP-GLCNAC'''<br />
 
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==Overview==
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==CRYSTAL STRUCTURE OF N-ACETYLGLUCOSAMINE 1-PHOSPHATE URIDYLTRANSFERASE BOUND TO UDP-GLCNAC==
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N-acetylglucosamine 1-phosphate uridyltransferase (GlmU) is a cytoplasmic, bifunctional enzyme involved in the biosynthesis of the, nucleotide-activated UDP-GlcNAc, which is an essential precursor for the, biosynthetic pathways of peptidoglycan and other components in bacteria., The crystal structure of a truncated form of GlmU has been solved at 2.25, A resolution using the multiwavelength anomalous dispersion technique and, its function tested with mutagenesis studies. The molecule is composed of, two distinct domains connected by a long alpha-helical arm: (i) an, N-terminal domain which resembles the dinucleotide-binding Rossmann fold;, and (ii) a C-terminal domain which adopts a left-handed parallel, beta-helix structure (LbetaH) as found in homologous bacterial, acetyltransferases. Three GlmU molecules assemble into a trimeric, arrangement with tightly packed parallel LbetaH domains, the long, alpha-helical linkers being seated on top of the arrangement and the, N-terminal domains projected away from the 3-fold axis. In addition, the, 2.3 A resolution structure of the GlmU-UDP-GlcNAc complex reveals the, structural bases required for the uridyltransferase activity. These, structures exemplify a three-dimensional template for the development of, new antibacterial agents and for studying other members of the large, family of XDP-sugar bacterial pyrophosphorylases.
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<StructureSection load='1fwy' size='340' side='right'caption='[[1fwy]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1fwy]] is a 2 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=1FWY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1FWY 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]] 2.3&#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=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=1fwy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fwy OCA], [https://pdbe.org/1fwy PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1fwy RCSB], [https://www.ebi.ac.uk/pdbsum/1fwy PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1fwy ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/GLMU_ECOLI GLMU_ECOLI] Catalyzes the last two sequential reactions in the de novo biosynthetic pathway for UDP-N-acetylglucosamine (UDP-GlcNAc). The C-terminal domain catalyzes the transfer of acetyl group from acetyl coenzyme A to glucosamine-1-phosphate (GlcN-1-P) to produce N-acetylglucosamine-1-phosphate (GlcNAc-1-P), which is converted into UDP-GlcNAc by the transfer of uridine 5-monophosphate (from uridine 5-triphosphate), a reaction catalyzed by the N-terminal domain.<ref>PMID:8083170</ref> <ref>PMID:8555230</ref>
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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/fw/1fwy_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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=1fwy ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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N-acetylglucosamine 1-phosphate uridyltransferase (GlmU) is a cytoplasmic bifunctional enzyme involved in the biosynthesis of the nucleotide-activated UDP-GlcNAc, which is an essential precursor for the biosynthetic pathways of peptidoglycan and other components in bacteria. The crystal structure of a truncated form of GlmU has been solved at 2.25 A resolution using the multiwavelength anomalous dispersion technique and its function tested with mutagenesis studies. The molecule is composed of two distinct domains connected by a long alpha-helical arm: (i) an N-terminal domain which resembles the dinucleotide-binding Rossmann fold; and (ii) a C-terminal domain which adopts a left-handed parallel beta-helix structure (LbetaH) as found in homologous bacterial acetyltransferases. Three GlmU molecules assemble into a trimeric arrangement with tightly packed parallel LbetaH domains, the long alpha-helical linkers being seated on top of the arrangement and the N-terminal domains projected away from the 3-fold axis. In addition, the 2.3 A resolution structure of the GlmU-UDP-GlcNAc complex reveals the structural bases required for the uridyltransferase activity. These structures exemplify a three-dimensional template for the development of new antibacterial agents and for studying other members of the large family of XDP-sugar bacterial pyrophosphorylases.
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==About this Structure==
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Crystal structure of the bifunctional N-acetylglucosamine 1-phosphate uridyltransferase from Escherichia coli: a paradigm for the related pyrophosphorylase superfamily.,Brown K, Pompeo F, Dixon S, Mengin-Lecreulx D, Cambillau C, Bourne Y EMBO J. 1999 Aug 2;18(15):4096-107. PMID:10428949<ref>PMID:10428949</ref>
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1FWY 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 SO4, UD1 and EDO as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/UDP-N-acetylglucosamine_diphosphorylase UDP-N-acetylglucosamine diphosphorylase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.7.23 2.7.7.23] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1FWY OCA].
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==Reference==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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Crystal structure of the bifunctional N-acetylglucosamine 1-phosphate uridyltransferase from Escherichia coli: a paradigm for the related pyrophosphorylase superfamily., Brown K, Pompeo F, Dixon S, Mengin-Lecreulx D, Cambillau C, Bourne Y, EMBO J. 1999 Aug 2;18(15):4096-107. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=10428949 10428949]
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</div>
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[[Category: Escherichia coli]]
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<div class="pdbe-citations 1fwy" style="background-color:#fffaf0;"></div>
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[[Category: Single protein]]
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[[Category: UDP-N-acetylglucosamine diphosphorylase]]
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[[Category: Bourne, Y.]]
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[[Category: Brown, K.]]
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[[Category: Cambillau, C.]]
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[[Category: Dixon, S.]]
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[[Category: Mengin-Lecreulx, D.]]
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[[Category: Pompeo, F.]]
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[[Category: EDO]]
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[[Category: SO4]]
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[[Category: UD1]]
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[[Category: acetyltransferase]]
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[[Category: bifunctional]]
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[[Category: crystallography]]
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[[Category: drug design]]
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[[Category: pyrophosphorylase]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 15:24:28 2007''
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==See Also==
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*[[N-acetylglucosamine-1-phosphate uridyltransferase|N-acetylglucosamine-1-phosphate uridyltransferase]]
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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: Escherichia coli]]
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[[Category: Large Structures]]
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[[Category: Bourne Y]]
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[[Category: Brown K]]
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[[Category: Cambillau C]]
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[[Category: Dixon S]]
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[[Category: Mengin-Lecreulx D]]
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[[Category: Pompeo F]]

Current revision

CRYSTAL STRUCTURE OF N-ACETYLGLUCOSAMINE 1-PHOSPHATE URIDYLTRANSFERASE BOUND TO UDP-GLCNAC

PDB ID 1fwy

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