2e3d

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[[Image:2e3d.jpg|left|200px]]
 
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==Crystal structure of E. coli glucose-1-phosphate uridylyltransferase==
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The line below this paragraph, containing "STRUCTURE_2e3d", creates the "Structure Box" on the page.
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<StructureSection load='2e3d' size='340' side='right'caption='[[2e3d]], [[Resolution|resolution]] 1.95&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'>[[2e3d]] is a 4 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=2E3D OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2E3D 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]] 1.95&#8491;</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=2e3d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2e3d OCA], [https://pdbe.org/2e3d PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2e3d RCSB], [https://www.ebi.ac.uk/pdbsum/2e3d PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2e3d ProSAT]</span></td></tr>
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{{STRUCTURE_2e3d| PDB=2e3d | SCENE= }}
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</table>
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== Function ==
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'''Crystal structure of E. coli glucose-1-phosphate uridylyltransferase'''
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[https://www.uniprot.org/uniprot/GALU_ECOLI GALU_ECOLI] May play a role in stationary phase survival.
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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==Overview==
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Check<jmol>
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Glucose-1-phosphate uridylyltransferase, also referred to as UDP-glucose pyrophosphorylase or UGPase, catalyzes the formation of UDP-glucose from glucose-1-phosphate and UTP. Not surprisingly, given the central role of UDP-glucose in glycogen synthesis and in the production of glycolipids, glycoproteins, and proteoglycans, the enzyme is ubiquitous in nature. Interestingly, however, the prokaryotic and eukaryotic forms of the enzyme are unrelated in amino acid sequence and structure. Here we describe the cloning and structural analysis to 1.9 A resolution of the UGPase from Escherichia coli. The protein is a tetramer with 222 point group symmetry. Each subunit of the tetramer is dominated by an eight-stranded mixed beta-sheet. There are two additional layers of beta-sheet (two and three strands) and 10 alpha-helices. The overall fold of the molecule is remarkably similar to that observed for glucose-1-phosphate thymidylyltransferase in complex with its product, dTDP-glucose. On the basis of this similarity, a UDP-glucose moiety has been positioned into the active site of UGPase. This protein/product model predicts that the side chains of Gln 109 and Asp 137, respectively, serve to anchor the uracil ring and the ribose of UDP-glucose to the protein. The beta-phosphoryl group of the product is predicted to lie within hydrogen bonding distance to the epsilon-nitrogen of Lys 202 whereas the carboxylate group of Glu 201 is predicted to bridge the 2'- and 3'-hydroxyl groups of the glucosyl moiety. Details concerning the overall structure of UGPase and a comparison with glucose-1-phosphate thymidylyltransferase are presented.
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/e3/2e3d_consurf.spt"</scriptWhenChecked>
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==About this Structure==
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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2E3D is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2E3D OCA].
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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==Reference==
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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=2e3d ConSurf].
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The molecular architecture of glucose-1-phosphate uridylyltransferase., Thoden JB, Holden HM, Protein Sci. 2007 Mar;16(3):432-40. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17322528 17322528]
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<div style="clear:both"></div>
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__TOC__
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</StructureSection>
[[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: UTP--glucose-1-phosphate uridylyltransferase]]
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[[Category: Holden HM]]
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[[Category: Holden, H M.]]
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[[Category: Thoden JB]]
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[[Category: Thoden, J B.]]
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[[Category: Carbohydrate]]
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[[Category: Pyrophosphorylase]]
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[[Category: Udp-glucose]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 01:50:58 2008''
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Current revision

Crystal structure of E. coli glucose-1-phosphate uridylyltransferase

PDB ID 2e3d

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