View source for 3kdy


==X-ray crystal structure of tyrosine aminomutase mutant construct==
<StructureSection load='3kdy' size='340' side='right'caption='[[3kdy]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[3kdy]] 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=3KDY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3KDY 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]] 2.2&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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=3kdy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3kdy OCA], [https://pdbe.org/3kdy PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3kdy RCSB], [https://www.ebi.ac.uk/pdbsum/3kdy PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3kdy 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/kd/3kdy_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=3kdy ConSurf].
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== Publication Abstract from PubMed ==
The tyrosine aminomutase SgTAM produces (S)-ss-tyrosine from L-tyrosine in the biosynthesis of the enediyne antitumor antibiotic C-1027. This conversion is promoted by the methylideneimidazole-5-one (MIO) prosthetic group. MIO was first identified in the homologous family of ammonia lyases, which deaminate aromatic amino acids to form alpha,ss-unsaturated carboxylates. Studies of substrate specificity have been described for lyases but there have been limited reports in altering the substrate specificity of aminomutases. Furthermore, it remains unclear as to what structural properties are responsible for catalyzing the presumed readdition of the amino group into the alpha,ss-unsaturated intermediates to form ss-amino acids. Attempts to elucidate specificity and mechanistic determinants of SgTAM have also proved to be difficult as it is recalcitrant to perturbations to the active site via mutagenesis. An X-ray cocrystal structure of the SgTAM mutant of the catalytic base with L-tyrosine verified important substrate binding residues as well as the enzymatic base. Further mutagenesis revealed that removal of these crucial interactions renders the enzyme inactive. Proposed structural determinants for mutase activity probed via mutagenesis, time-point assays and X-ray crystallography revealed a complicated role for these residues in maintaining key quaternary structure properties that aid in catalysis. (c) 2010 Wiley Periodicals, Inc. Biopolymers 93: 802-810, 2010.

Probing the active site of MIO-dependent aminomutases, key catalysts in the biosynthesis of beta-amino acids incorporated in secondary metabolites.,Cooke HA, Bruner SD Biopolymers. 2010 Sep;93(9):802-10. PMID:20577998<ref>PMID:20577998</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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<div class="pdbe-citations 3kdy" style="background-color:#fffaf0;"></div>

==See Also==
*[[Aminomutase 3D structures|Aminomutase 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Streptomyces globisporus]]
[[Category: Bruner SD]]
[[Category: Cooke HA]]