6on3: Difference between revisions
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<StructureSection load='6on3' size='340' side='right'caption='[[6on3]], [[Resolution|resolution]] 2.31Å' scene=''> | <StructureSection load='6on3' size='340' side='right'caption='[[6on3]], [[Resolution|resolution]] 2.31Å' scene=''> | ||
== Structural highlights == | == 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> | <table><tr><td colspan='2'>[[6on3]] 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=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> | </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> | <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> | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Atcc 15721]] | |||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Colabroy, K]] | [[Category: Colabroy, K]] | ||
Revision as of 12:08, 27 November 2019
A substrate bound structure of L-DOPA dioxygenase from Streptomyces sclerotialusA substrate bound structure of L-DOPA dioxygenase from Streptomyces sclerotialus
Structural highlights
Publication Abstract from PubMedExtradiol 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. 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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