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| ==Crystal Structure of AviO1 from Streptomyces viridochromogenes Tue57== | | ==Crystal Structure of AviO1 from Streptomyces viridochromogenes Tue57== |
| <StructureSection load='4xaa' size='340' side='right' caption='[[4xaa]], [[Resolution|resolution]] 2.30Å' scene=''> | | <StructureSection load='4xaa' size='340' side='right'caption='[[4xaa]], [[Resolution|resolution]] 2.30Å' scene=''> |
| == Structural highlights == | | == Structural highlights == |
| <table><tr><td colspan='2'>[[4xaa]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4XAA OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4XAA FirstGlance]. <br> | | <table><tr><td colspan='2'>[[4xaa]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptomyces_viridochromogenes_Tue57 Streptomyces viridochromogenes Tue57]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4XAA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4XAA FirstGlance]. <br> |
| </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NI:NICKEL+(II)+ION'>NI</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]] 2.3Å</td></tr> |
| <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4xab|4xab]], [[4xac|4xac]]</td></tr> | | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NI:NICKEL+(II)+ION'>NI</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=4xaa FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4xaa OCA], [http://pdbe.org/4xaa PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4xaa RCSB], [http://www.ebi.ac.uk/pdbsum/4xaa PDBsum]</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=4xaa FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4xaa OCA], [https://pdbe.org/4xaa PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4xaa RCSB], [https://www.ebi.ac.uk/pdbsum/4xaa PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4xaa ProSAT]</span></td></tr> |
| </table> | | </table> |
| <div style="background-color:#fffaf0;">
| | == Function == |
| == Publication Abstract from PubMed == | | [https://www.uniprot.org/uniprot/Q93KW4_STRVR Q93KW4_STRVR] |
| Orthosomycins are oligosaccharide antibiotics that include avilamycin, everninomicin, and hygromycin B and are hallmarked by a rigidifying interglycosidic spirocyclic ortho-delta-lactone (orthoester) linkage between at least one pair of carbohydrates. A subset of orthosomycins additionally contain a carbohydrate capped by a methylenedioxy bridge. The orthoester linkage is necessary for antibiotic activity but rarely observed in natural products. Orthoester linkage and methylenedioxy bridge biosynthesis require similar oxidative cyclizations adjacent to a sugar ring. We have identified a conserved group of nonheme iron, alpha-ketoglutarate-dependent oxygenases likely responsible for this chemistry. High-resolution crystal structures of the EvdO1 and EvdO2 oxygenases of everninomicin biosynthesis, the AviO1 oxygenase of avilamycin biosynthesis, and HygX of hygromycin B biosynthesis show how these enzymes accommodate large substrates, a challenge that requires a variation in metal coordination in HygX. Excitingly, the ternary complex of HygX with cosubstrate alpha-ketoglutarate and putative product hygromycin B identified an orientation of one glycosidic linkage of hygromycin B consistent with metal-catalyzed hydrogen atom abstraction from substrate. These structural results are complemented by gene disruption of the oxygenases evdO1 and evdMO1 from the everninomicin biosynthetic cluster, which demonstrate that functional oxygenase activity is critical for antibiotic production. Our data therefore support a role for these enzymes in the production of key features of the orthosomycin antibiotics.
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| Oxidative cyclizations in orthosomycin biosynthesis expand the known chemistry of an oxygenase superfamily.,McCulloch KM, McCranie EK, Smith JA, Sarwar M, Mathieu JL, Gitschlag BL, Du Y, Bachmann BO, Iverson TM Proc Natl Acad Sci U S A. 2015 Aug 3. pii: 201500964. PMID:26240321<ref>PMID:26240321</ref>
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| From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
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| </div>
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| <div class="pdbe-citations 4xaa" style="background-color:#fffaf0;"></div>
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| == References ==
| |
| <references/>
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| __TOC__ | | __TOC__ |
| </StructureSection> | | </StructureSection> |
| [[Category: Bachmann, B O]] | | [[Category: Large Structures]] |
| [[Category: Du, Y]] | | [[Category: Streptomyces viridochromogenes Tue57]] |
| [[Category: Gitschlag, B L]] | | [[Category: Bachmann BO]] |
| [[Category: Iverson, T M]] | | [[Category: Du Y]] |
| [[Category: Mathieu, J L]] | | [[Category: Gitschlag BL]] |
| [[Category: McCranie, E K]] | | [[Category: Iverson TM]] |
| [[Category: McCulloch, K M]] | | [[Category: Mathieu JL]] |
| [[Category: Sarwar, M]] | | [[Category: McCranie EK]] |
| [[Category: Double stranded beta helix]] | | [[Category: McCulloch KM]] |
| [[Category: Oxidoreductase]] | | [[Category: Sarwar M]] |