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| | ==OxyS anhydrotetracycline hydroxylase from Streptomyces rimosus== | | ==OxyS anhydrotetracycline hydroxylase from Streptomyces rimosus== |
| - | <StructureSection load='4k2x' size='340' side='right' caption='[[4k2x]], [[Resolution|resolution]] 2.55Å' scene=''> | + | <StructureSection load='4k2x' size='340' side='right'caption='[[4k2x]], [[Resolution|resolution]] 2.55Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4k2x]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Streptomyces_rimosus_subsp._rimosus_atcc_10970 Streptomyces rimosus subsp. rimosus atcc 10970]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4K2X OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4K2X FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4k2x]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptomyces_rimosus_subsp._rimosus_ATCC_10970 Streptomyces rimosus subsp. rimosus ATCC 10970]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4K2X OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4K2X FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</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]] 2.55Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">oxyS, SRIM_10936 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1265868 Streptomyces rimosus subsp. rimosus ATCC 10970])</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</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=4k2x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4k2x OCA], [http://pdbe.org/4k2x PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4k2x RCSB], [http://www.ebi.ac.uk/pdbsum/4k2x PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4k2x 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=4k2x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4k2x OCA], [https://pdbe.org/4k2x PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4k2x RCSB], [https://www.ebi.ac.uk/pdbsum/4k2x PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4k2x ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/OXYS_STRR1 OXYS_STRR1] Involved in the biosynthesis of the antibiotics oxytetracycline and tetracycline. OxyS starts by catalyzing the stereospecific hydroxylation of anhydrotetracycline at C(6) position to yield 5a,11a-dehydrotetracycline (12-dehydrotetracycline). If the released product is captured by OxyR, it is reduced to tetracycline. However, if the released product is recaptured by OxyS, it performs an additional hydroxylation at C(5), producing 5a,11a-dehydrooxytetracycline, which, following the action of OxyR becomes oxytetracycline.<ref>PMID:23621493</ref> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Streptomyces rimosus subsp. rimosus atcc 10970]] | + | [[Category: Large Structures]] |
| - | [[Category: Sawaya, M R]] | + | [[Category: Streptomyces rimosus subsp. rimosus ATCC 10970]] |
| - | [[Category: Tang, Y]] | + | [[Category: Sawaya MR]] |
| - | [[Category: Wang, P]] | + | [[Category: Tang Y]] |
| - | [[Category: Fad binding]]
| + | [[Category: Wang P]] |
| - | [[Category: Flavoprotein]]
| + | |
| - | [[Category: Hydroxylase]]
| + | |
| - | [[Category: Oxidoreductase]]
| + | |
| - | [[Category: Para-hydroxybenzoate hydroxylase fold]]
| + | |
| Structural highlights
Function
OXYS_STRR1 Involved in the biosynthesis of the antibiotics oxytetracycline and tetracycline. OxyS starts by catalyzing the stereospecific hydroxylation of anhydrotetracycline at C(6) position to yield 5a,11a-dehydrotetracycline (12-dehydrotetracycline). If the released product is captured by OxyR, it is reduced to tetracycline. However, if the released product is recaptured by OxyS, it performs an additional hydroxylation at C(5), producing 5a,11a-dehydrooxytetracycline, which, following the action of OxyR becomes oxytetracycline.[1]
Publication Abstract from PubMed
Tetracyclines are a group of natural products sharing a linearly fused four-ring scaffold, which is essential for their broad-spectrum antibiotic activities. Formation of the key precursor anhydrotetracycline 3 during oxytetracycline 1 biosynthesis has been previously characterized. However, the enzymatic steps that transform 3 into 1, including the additional hydroxylation at C5 and the final C5a-C11a reduction, have remained elusive. Here we report two redox enzymes, OxyS and OxyR, are sufficient to convert 3 to 1. OxyS catalyzes two sequential hydroxylations at C6 and C5 positions of 3 with opposite stereochemistry, while OxyR catalyzes the C5a-C11a reduction using F420 as a cofactor to produce 1. The crystal structure of OxyS was obtained to provide insights into the tandem C6- and C5-hydroxylation steps. The substrate specificities of OxyS and OxyR were shown to influence the relative ratio of 1 and tetracycline 2.
Uncovering the Enzymes that Catalyze the Final Steps in Oxytetracycline Biosynthesis.,Wang P, Bashiri G, Gao X, Sawaya MR, Tang Y J Am Chem Soc. 2013 May 15;135(19):7138-7141. Epub 2013 May 1. PMID:23621493[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Wang P, Bashiri G, Gao X, Sawaya MR, Tang Y. Uncovering the Enzymes that Catalyze the Final Steps in Oxytetracycline Biosynthesis. J Am Chem Soc. 2013 May 15;135(19):7138-7141. Epub 2013 May 1. PMID:23621493 doi:10.1021/ja403516u
- ↑ Wang P, Bashiri G, Gao X, Sawaya MR, Tang Y. Uncovering the Enzymes that Catalyze the Final Steps in Oxytetracycline Biosynthesis. J Am Chem Soc. 2013 May 15;135(19):7138-7141. Epub 2013 May 1. PMID:23621493 doi:10.1021/ja403516u
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