4k2x
From Proteopedia
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| - | + | ==OxyS anhydrotetracycline hydroxylase from Streptomyces rimosus== | |
| - | === | + | <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 [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> | ||
| + | </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> | ||
| + | <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='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://www.rcsb.org/pdb/explore.do?structureId=4k2x RCSB], [http://www.ebi.ac.uk/pdbsum/4k2x PDBsum]</span></td></tr> | ||
| + | </table> | ||
| + | <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> | |
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
[[Category: Streptomyces rimosus subsp. rimosus atcc 10970]] | [[Category: Streptomyces rimosus subsp. rimosus atcc 10970]] | ||
| - | [[Category: Sawaya, M R | + | [[Category: Sawaya, M R]] |
| - | [[Category: Tang, Y | + | [[Category: Tang, Y]] |
| - | [[Category: Wang, P | + | [[Category: Wang, P]] |
[[Category: Fad binding]] | [[Category: Fad binding]] | ||
[[Category: Flavoprotein]] | [[Category: Flavoprotein]] | ||
Revision as of 14:52, 21 December 2014
OxyS anhydrotetracycline hydroxylase from Streptomyces rimosus
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