4lei

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==Spinosyn Forosaminyltransferase SpnP==
==Spinosyn Forosaminyltransferase SpnP==
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<StructureSection load='4lei' size='340' side='right' caption='[[4lei]], [[Resolution|resolution]] 3.15&Aring;' scene=''>
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<StructureSection load='4lei' size='340' side='right'caption='[[4lei]], [[Resolution|resolution]] 3.15&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[4lei]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4LEI OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4LEI FirstGlance]. <br>
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<table><tr><td colspan='2'>[[4lei]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharopolyspora_spinosa Saccharopolyspora spinosa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4LEI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4LEI FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=TYD:THYMIDINE-5-DIPHOSPHATE'>TYD</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.15&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4ldp|4ldp]]</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=TYD:THYMIDINE-5-DIPHOSPHATE'>TYD</scene></td></tr>
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<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=4lei FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4lei OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4lei RCSB], [http://www.ebi.ac.uk/pdbsum/4lei PDBsum]</span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4lei FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4lei OCA], [https://pdbe.org/4lei PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4lei RCSB], [https://www.ebi.ac.uk/pdbsum/4lei PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4lei ProSAT]</span></td></tr>
</table>
</table>
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<div style="background-color:#fffaf0;">
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== Function ==
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== Publication Abstract from PubMed ==
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[https://www.uniprot.org/uniprot/Q9ALN7_SACSN Q9ALN7_SACSN]
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Spinosyns A and D (spinosad) are complex polyketide natural products biosynthesized through the cooperation of a modular polyketide synthase and several tailoring enzymes. SpnP catalyzes the final tailoring step, transferring forosamine from a TDP-D-forosamine donor substrate to a spinosyn pseudoaglycone acceptor substrate. Sequence analysis indicated that SpnP belongs to a small group of glycosyltransferases (GTs) that require an auxiliary protein for activation. However, unlike other GTs in this subgroup, no putative auxiliary protein gene could be located in the biosynthetic gene cluster. To learn more about SpnP, the structures of SpnP and its complex with TDP were determined to 2.50 and 3.15 A resolution, respectively. Binding of TDP causes the reordering of several residues in the donor substrate pocket. SpnP possesses a structural feature that has only been previously observed in the related glycosyltransferase EryCIII, in which it mediates association with the auxiliary protein EryCII. This motif, H-X-R-X5-D-X5-R-X12-20-D-P-X3-W-L-X12-18-E-X4-G, may be predictive of glycosyltransferases that interact with an auxiliary protein. A reverse glycosyl transfer assay demonstrated that SpnP possesses measurable activity in the absence of an auxiliary protein. Our data suggest that SpnP can bind its donor substrate by itself but that the glycosyl transfer reaction is facilitated by an auxiliary protein that aids in the correct folding of a flexible loop surrounding the pseudoaglycone acceptor substrate-binding pocket.
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Structural studies of the spinosyn forosaminyltransferase, SpnP.,Isiorho EA, Jeon BS, Kim NH, Liu HW, Keatinge-Clay AT Biochemistry. 2014 Jul 8;53(26):4292-301. doi: 10.1021/bi5003629. Epub 2014 Jun, 26. PMID:24945604<ref>PMID:24945604</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Isiorho, E A]]
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[[Category: Large Structures]]
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[[Category: Keatinge-Clay, A K]]
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[[Category: Saccharopolyspora spinosa]]
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[[Category: Liu, H W]]
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[[Category: Isiorho EA]]
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[[Category: Glycosyltransferase]]
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[[Category: Keatinge-Clay AK]]
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[[Category: Transferase]]
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[[Category: Liu H-W]]

Current revision

Spinosyn Forosaminyltransferase SpnP

PDB ID 4lei

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