2rjr
From Proteopedia
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| - | [[Image:2rjr.jpg|left|200px]]<br /><applet load="2rjr" size="350" color="white" frame="true" align="right" spinBox="true" | ||
| - | caption="2rjr, resolution 2.100Å" /> | ||
| - | '''Substrate mimic bound to SgTAM'''<br /> | ||
| - | == | + | ==Substrate mimic bound to SgTAM== |
| + | <StructureSection load='2rjr' size='340' side='right'caption='[[2rjr]], [[Resolution|resolution]] 2.10Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[2rjr]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptomyces_globisporus Streptomyces globisporus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2RJR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2RJR 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]] 2.1Å</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=295:(2S,3S)-3-(4-FLUOROPHENYL)-2,3-DIHYDROXYPROPANOIC+ACID'>295</scene>, <scene name='pdbligand=MDO:{2-[(1S)-1-AMINOETHYL]-4-METHYLIDENE-5-OXO-4,5-DIHYDRO-1H-IMIDAZOL-1-YL}ACETIC+ACID'>MDO</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=2rjr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2rjr OCA], [https://pdbe.org/2rjr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2rjr RCSB], [https://www.ebi.ac.uk/pdbsum/2rjr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2rjr ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/TAM_STRGL TAM_STRGL] Involved in the biosynthesis of the enediyne antitumor antibiotic C-1027. Catalyzes the MIO-dependent deamination of L-tyrosine generating the corresponding alpha,beta-unsaturated acid, (S)-beta-tyrosine.<ref>PMID:12183628</ref> <ref>PMID:17516659</ref> <ref>PMID:20577998</ref> | ||
| + | == 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/rj/2rjr_consurf.spt"</scriptWhenChecked> | ||
| + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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=2rjr ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
The synthesis and evaluation of two classes of inhibitors for SgTAM, a 4-methylideneimidazole-5-one (MIO) containing tyrosine aminomutase, are described. A mechanism-based strategy was used to design analogs that mimic the substrate or product of the reaction and form covalent interactions with the enzyme through the MIO prosthetic group. The analogs were characterized by measuring inhibition constants and X-ray crystallographic structural analysis of the co-complexes bound to the aminomutase, SgTAM. | The synthesis and evaluation of two classes of inhibitors for SgTAM, a 4-methylideneimidazole-5-one (MIO) containing tyrosine aminomutase, are described. A mechanism-based strategy was used to design analogs that mimic the substrate or product of the reaction and form covalent interactions with the enzyme through the MIO prosthetic group. The analogs were characterized by measuring inhibition constants and X-ray crystallographic structural analysis of the co-complexes bound to the aminomutase, SgTAM. | ||
| - | + | Design and characterization of mechanism-based inhibitors for the tyrosine aminomutase SgTAM.,Montavon TJ, Christianson CV, Festin GM, Shen B, Bruner SD Bioorg Med Chem Lett. 2008 May 15;18(10):3099-102. Epub 2007 Nov 19. PMID:18078753<ref>PMID:18078753</ref> | |
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| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | <div class="pdbe-citations 2rjr" style="background-color:#fffaf0;"></div> | |
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| - | + | ==See Also== | |
| + | *[[Aminomutase 3D structures|Aminomutase 3D structures]] | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Streptomyces globisporus]] | ||
| + | [[Category: Bruner SD]] | ||
| + | [[Category: Christianson CV]] | ||
| + | [[Category: Montavon TJ]] | ||
Current revision
Substrate mimic bound to SgTAM
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