4k2x
From Proteopedia
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- | {{STRUCTURE_4k2x| PDB=4k2x | SCENE= }} | ||
- | ===OxyS anhydrotetracycline hydroxylase from Streptomyces rimosus=== | ||
- | {{ABSTRACT_PUBMED_23621493}} | ||
- | == | + | ==OxyS anhydrotetracycline hydroxylase from Streptomyces rimosus== |
- | [[4k2x]] is a 2 chain structure with sequence from [ | + | <StructureSection load='4k2x' size='340' side='right'caption='[[4k2x]], [[Resolution|resolution]] 2.55Å' scene=''> |
- | [ | + | == Structural highlights == |
- | [[ | + | <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='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='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> |
- | [[Category: | + | <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> |
- | [[Category: | + | </table> |
- | [[Category: | + | == Function == |
- | [[Category: | + | [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> |
- | [[Category: | + | <div style="background-color:#fffaf0;"> |
+ | == 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<ref>PMID:23621493</ref> | ||
+ | |||
+ | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
+ | </div> | ||
+ | <div class="pdbe-citations 4k2x" style="background-color:#fffaf0;"></div> | ||
+ | == References == | ||
+ | <references/> | ||
+ | __TOC__ | ||
+ | </StructureSection> | ||
+ | [[Category: Large Structures]] | ||
+ | [[Category: Streptomyces rimosus subsp. rimosus ATCC 10970]] | ||
+ | [[Category: Sawaya MR]] | ||
+ | [[Category: Tang Y]] | ||
+ | [[Category: Wang P]] |
Current revision
OxyS anhydrotetracycline hydroxylase from Streptomyces rimosus
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