6on1: Difference between revisions

<table><tr><td colspan='2'>[[6on1]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_15721 Atcc 15721]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6ON1 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6ON1 FirstGlance]. <br>

</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FE:FE+(III)+ION'>FE</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=6on1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6on1 OCA], [http://pdbe.org/6on1 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6on1 RCSB], [http://www.ebi.ac.uk/pdbsum/6on1 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6on1 ProSAT]</span></td></tr>

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== 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.

 

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== References ==

[[Category: Colabroy, K]]

[[Category: Fu, Y]]

[[Category: Liu, A]]

[[Category: Shin, I]]

[[Category: Wang, Y]]

[[Category: Vincinal oxygen chelate superfamily]]