6on3: Difference between revisions

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'''Unreleased structure'''


The entry 6on3 is ON HOLD  until Paper Publication
==A substrate bound structure of L-DOPA dioxygenase from Streptomyces sclerotialus==
<StructureSection load='6on3' size='340' side='right'caption='[[6on3]], [[Resolution|resolution]] 2.31&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[6on3]] is a 6 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6ON3 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6ON3 FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=DAH:3,4-DIHYDROXYPHENYLALANINE'>DAH</scene>, <scene name='pdbligand=FE2:FE+(II)+ION'>FE2</scene>, <scene name='pdbligand=TRS:2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>TRS</scene></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6on3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6on3 OCA], [http://pdbe.org/6on3 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6on3 RCSB], [http://www.ebi.ac.uk/pdbsum/6on3 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6on3 ProSAT]</span></td></tr>
</table>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Extradiol dioxygenases are essential biocatalysts to breakdown catechols. The vicinal oxygen chelate (VOC) superfamily contains a large number of extradiol dioxygenases, most of which are found as part of catabolic pathways degrading a variety of natural and human-made aromatic rings. However, the VOC also contains an emerging class of biosynthetic dioxygenases. The L-3,4-dihydroxyphenylalanine (L-DOPA) extradiol dioxygenases are from pathways to various antibacterial or antitumor natural products, and their structural features are anticipated to be distinct from other VOC extradiol dioxygenases. Herein, we identified a new L-DOPA dioxygenase from the thermophilic bacterium Streptomyces sclerotialus (SsDDO), through a sequence and genome context analysis. The activity of SsDDO was kinetically characterized with L-DOPA using a UV-vis spectrophotometer and an oxygen electrode. The optimal temperature of the assay was 55 C, at which the Km and kcat of SsDDO were 110 +/- 10 muM and 2.0 +/- 0.1 s-1, respectively. We determined the de novo crystal structures of SsDDO in both the ligand-free form and as a substrate-bound complex, refined to 1.99 A and 2.31 A resolution, respectively. These structures reveal that SsDDO possesses a Form IV arrangement of betaalphabetabetabeta modules, the first characterization of this assembly from among the VOC/Type I extradiol dioxygenase protein family. EPR spectra of Fe-NO adducts for the resting and substrate-bound enzyme were obtained. This work contributes to our understanding of a growing class of topologically distinct VOC dioxygenases, and the obtained structural features will expand our knowledge of the extradiol cleavage reaction within the VOC superfamily.


Authors: Wang, Y., Shin, I., Fu, Y., Colabroy, K., Liu, A.
Crystal Structures of L-DOPA Dioxygenase from Streptomyces Sclerotialus.,Wang Y, Shin I, Fu Y, Colabroy KL, Liu A Biochemistry. 2019 Jun 10. doi: 10.1021/acs.biochem.9b00396. PMID:31180203<ref>PMID:31180203</ref>


Description: A substrate bound structure of L-DOPA dioxygenase from Streptomyces sclerotialus
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
[[Category: Unreleased Structures]]
</div>
<div class="pdbe-citations 6on3" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Colabroy, K]]
[[Category: Colabroy, K]]
[[Category: Fu, Y]]
[[Category: Fu, Y]]
[[Category: Wang, Y]]
[[Category: Liu, A]]
[[Category: Liu, A]]
[[Category: Shin, I]]
[[Category: Shin, I]]
[[Category: Wang, Y]]
[[Category: Extradiol dioxygenase]]
[[Category: Oxidoreductase]]
[[Category: Vincinal oxygen chelate superfamily]]

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