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| | <StructureSection load='2qve' size='340' side='right'caption='[[2qve]], [[Resolution|resolution]] 2.00Å' scene=''> | | <StructureSection load='2qve' size='340' side='right'caption='[[2qve]], [[Resolution|resolution]] 2.00Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2qve]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/"actinomyces_globisporus"_krasil'nikov_1941 "actinomyces globisporus" krasil'nikov 1941]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2QVE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2QVE FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2qve]] 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=2QVE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2QVE FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=247:(3R)-3-AMINO-2,2-DIFLUORO-3-(4-HYDROXYPHENYL)PROPANOIC+ACID'>247</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2Å</td></tr> |
| - | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><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='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=247:(3R)-3-AMINO-2,2-DIFLUORO-3-(4-HYDROXYPHENYL)PROPANOIC+ACID'>247</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='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2ohy|2ohy]]</div></td></tr>
| + | |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Tyrosine_2,3-aminomutase Tyrosine 2,3-aminomutase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.4.3.6 5.4.3.6] </span></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=2qve FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2qve OCA], [https://pdbe.org/2qve PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2qve RCSB], [https://www.ebi.ac.uk/pdbsum/2qve PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2qve ProSAT]</span></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=2qve FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2qve OCA], [https://pdbe.org/2qve PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2qve RCSB], [https://www.ebi.ac.uk/pdbsum/2qve PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2qve ProSAT]</span></td></tr> |
| | </table> | | </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 == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Actinomyces globisporus krasil'nikov 1941]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Tyrosine 2,3-aminomutase]] | + | [[Category: Streptomyces globisporus]] |
| - | [[Category: Bruner, S D]] | + | [[Category: Bruner SD]] |
| - | [[Category: Christianson, C V]] | + | [[Category: Christianson CV]] |
| - | [[Category: Montavon, T J]] | + | [[Category: Montavon TJ]] |
| - | [[Category: Aminomutase]]
| + | |
| - | [[Category: Enediyne]]
| + | |
| - | [[Category: Mio]]
| + | |
| - | [[Category: Transferase]]
| + | |
| Structural highlights
Function
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.[1] [2] [3]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
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.
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[4]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Liu W, Christenson SD, Standage S, Shen B. Biosynthesis of the enediyne antitumor antibiotic C-1027. Science. 2002 Aug 16;297(5584):1170-3. PMID:12183628 doi:10.1126/science.1072110
- ↑ Christianson CV, Montavon TJ, Van Lanen SG, Shen B, Bruner SD. The structure of L-tyrosine 2,3-aminomutase from the C-1027 enediyne antitumor antibiotic biosynthetic pathway. Biochemistry. 2007 Jun 19;46(24):7205-14. Epub 2007 May 22. PMID:17516659 doi:10.1021/bi7003685
- ↑ Cooke HA, Bruner SD. Probing the active site of MIO-dependent aminomutases, key catalysts in the biosynthesis of beta-amino acids incorporated in secondary metabolites. Biopolymers. 2010 Sep;93(9):802-10. PMID:20577998 doi:10.1002/bip.21500
- ↑ Montavon TJ, Christianson CV, Festin GM, Shen B, Bruner SD. Design and characterization of mechanism-based inhibitors for the tyrosine aminomutase SgTAM. Bioorg Med Chem Lett. 2008 May 15;18(10):3099-102. Epub 2007 Nov 19. PMID:18078753 doi:10.1016/j.bmcl.2007.11.046
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