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2ihu

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(New page: 200px<br /><applet load="2ihu" size="350" color="white" frame="true" align="right" spinBox="true" caption="2ihu, resolution 2.05&Aring;" /> '''Carboxyethylarginine...)
Current revision (10:11, 30 August 2023) (edit) (undo)
 
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[[Image:2ihu.jpg|left|200px]]<br /><applet load="2ihu" size="350" color="white" frame="true" align="right" spinBox="true"
 
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caption="2ihu, resolution 2.05&Aring;" />
 
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'''Carboxyethylarginine synthase from Streptomyces clavuligerus: putative reaction intermediate complex'''<br />
 
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==About this Structure==
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==Carboxyethylarginine synthase from Streptomyces clavuligerus: putative reaction intermediate complex==
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2IHU is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Streptomyces_clavuligerus Streptomyces clavuligerus] with <scene name='pdbligand=MG:'>MG</scene>, <scene name='pdbligand=K:'>K</scene>, <scene name='pdbligand=TP9:'>TP9</scene>, <scene name='pdbligand=TP8:'>TP8</scene>, <scene name='pdbligand=TAR:'>TAR</scene> and <scene name='pdbligand=GOL:'>GOL</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/N(2)-(2-carboxyethyl)arginine_synthase N(2)-(2-carboxyethyl)arginine synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.5.1.66 2.5.1.66] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2IHU OCA].
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<StructureSection load='2ihu' size='340' side='right'caption='[[2ihu]], [[Resolution|resolution]] 2.05&Aring;' scene=''>
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[[Category: N(2)-(2-carboxyethyl)arginine synthase]]
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== Structural highlights ==
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[[Category: Single protein]]
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<table><tr><td colspan='2'>[[2ihu]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptomyces_clavuligerus Streptomyces clavuligerus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2IHU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2IHU FirstGlance]. <br>
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[[Category: Streptomyces clavuligerus]]
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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]] 2.05&#8491;</td></tr>
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[[Category: Caines, M.E.C.]]
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=TAR:D(-)-TARTARIC+ACID'>TAR</scene>, <scene name='pdbligand=TP8:5-(2-{[HYDROXY(PHOSPHONOOXY)PHOSPHORYL]OXY}ETHYL)-2-[(1Z)-1-HYDROXY-3-(PHOSPHONOOXY)PROP-1-EN-1-YL]-3-{[(4Z)-4-IMINO-2-METHYL-4,5-DIHYDROPYRIMIDIN-5-YL]METHYL}-4-METHYL-1,3-THIAZOL-3-IUM'>TP8</scene>, <scene name='pdbligand=TP9:(3Z)-4-{[(4-AMINO-2-METHYLPYRIMIDIN-5-YL)METHYL]AMINO}-3-MERCAPTOPENT-3-EN-1-YL+TRIHYDROGEN+DIPHOSPHATE'>TP9</scene></td></tr>
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[[Category: Schofield, C.J.]]
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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=2ihu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ihu OCA], [https://pdbe.org/2ihu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2ihu RCSB], [https://www.ebi.ac.uk/pdbsum/2ihu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2ihu ProSAT]</span></td></tr>
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[[Category: GOL]]
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</table>
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[[Category: K]]
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== Function ==
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[[Category: MG]]
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[https://www.uniprot.org/uniprot/CEAS_STRCL CEAS_STRCL] Involved in the biosynthesis of the beta-lactamase inhibitor, clavulanic acid. Catalyzes the thiamine diphosphate (ThDP) dependent condensation of D-glyceraldehyde-3-phosphate (D-G3P) with L-arginine to yield the beta-amino acid, N2-(2-carboxyethyl)arginine (CEA) via a beta-elimination resulting in the formation of an enol which undergoes a second elimination to generate the alpha,beta-unsaturated acryloyl-ThDP.<ref>PMID:18052280</ref> <ref>PMID:19477162</ref>
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[[Category: TAR]]
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== Evolutionary Conservation ==
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[[Category: TP8]]
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[[Image:Consurf_key_small.gif|200px|right]]
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[[Category: TP9]]
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Check<jmol>
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[[Category: thiamin diphosphate complex]]
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<jmolCheckbox>
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[[Category: transferase]]
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ih/2ihu_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=2ihu 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(2)-(2-Carboxyethyl)arginine synthase (CEAS), an unusual thiamin diphosphate (ThDP)-dependent enzyme, catalyses the committed step in the biosynthesis of the b-lactamase inhibitor clavulanic acid in Streptomyces clavuligerus. Crystal structures of tetrameric CEAS-ThDP in complex with the substrate analogues 5-guanidinovaleric acid (GVA) and tartrate, and a structure reflecting a possible enol(ate)-ThDP reaction intermediate are described. The structures suggest overlapping binding sites for the substrates D-glyceraldehyde-3-phosphate (D-G3P) and L-arginine, and are consistent with the proposed CEAS mechanism in which D-G3P binds at the active site and reacts to form an alpha,beta-unsaturated intermediate,which subsequently undergoes (1,4)-Michael addition with the alpha-amino group of L-arginine. Additional solution studies are presented which probe the amino acid substrate tolerance of CEAS, providing further insight into the L-arginine binding site. These findings may facilitate the engineering of CEAS towards the synthesis of alternative beta-amino acid products.
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jan 23 11:58:07 2008''
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Structural and mechanistic studies on N(2)-(2-carboxyethyl)arginine synthase.,Caines ME, Sorensen JL, Schofield CJ Biochem Biophys Res Commun. 2009 Aug 7;385(4):512-7. Epub 2009 May 27. PMID:19477162<ref>PMID:19477162</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 2ihu" style="background-color:#fffaf0;"></div>
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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: Large Structures]]
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[[Category: Streptomyces clavuligerus]]
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[[Category: Caines ME]]
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[[Category: Schofield CJ]]

Current revision

Carboxyethylarginine synthase from Streptomyces clavuligerus: putative reaction intermediate complex

PDB ID 2ihu

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