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3tsa

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Current revision (13:37, 14 March 2024) (edit) (undo)
 
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<StructureSection load='3tsa' size='340' side='right'caption='[[3tsa]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
<StructureSection load='3tsa' size='340' side='right'caption='[[3tsa]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[3tsa]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Atcc_49460 Atcc 49460]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3TSA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3TSA FirstGlance]. <br>
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<table><tr><td colspan='2'>[[3tsa]] 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=3TSA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3TSA FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GLC:ALPHA-D-GLUCOSE'>GLC</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</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]] 1.7&#8491;</td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">spnG ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=60894 ATCC 49460])</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=GLC:ALPHA-D-GLUCOSE'>GLC</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></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=3tsa FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3tsa OCA], [https://pdbe.org/3tsa PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3tsa RCSB], [https://www.ebi.ac.uk/pdbsum/3tsa PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3tsa 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=3tsa FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3tsa OCA], [https://pdbe.org/3tsa PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3tsa RCSB], [https://www.ebi.ac.uk/pdbsum/3tsa PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3tsa 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/Q9ALM8_SACSN Q9ALM8_SACSN]
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Spinosyns A and D (spinosad), like many other complex polyketides, are tailored near the end of their biosyntheses through the addition of sugars. SpnG, which catalyzes their 9-OH rhamnosylation, is also capable of adding other monosaccharides to the spinosyn aglycone (AGL) from TDP-sugars; however, the substitution of UDP-d-glucose for TDP-d-glucose as the donor substrate is known to result in a &gt;60000-fold reduction in k(cat). Here, we report the structure of SpnG at 1.65 A resolution, SpnG bound to TDP at 1.86 A resolution, and SpnG bound to AGL at 1.70 A resolution. The SpnG-TDP complex reveals how SpnG employs N202 to discriminate between TDP- and UDP-sugars. A conformational change of several residues in the active site is promoted by the binding of TDP. The SpnG-AGL complex shows that the binding of AGL is mediated via hydrophobic interactions and that H13, the potential catalytic base, is within 3 A of the nucleophilic 9-OH group of AGL. A model for the Michaelis complex was constructed to reveal the features that allow SpnG to transfer diverse sugars; it also revealed that the rhamnosyl moiety is in a skew-boat conformation during the transfer reaction.
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Structural Studies of the Spinosyn Rhamnosyltransferase, SpnG.,Isiorho EA, Liu HW, Keatinge-Clay AT Biochemistry. 2012 Feb 14;51(6):1213-22. Epub 2012 Feb 3. PMID:22283226<ref>PMID:22283226</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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<div class="pdbe-citations 3tsa" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Atcc 49460]]
 
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Isiorho, E A]]
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[[Category: Saccharopolyspora spinosa]]
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[[Category: Keatinge-Clay, A T]]
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[[Category: Isiorho EA]]
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[[Category: Liu, H W]]
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[[Category: Keatinge-Clay AT]]
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[[Category: Glycosyltransferase]]
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[[Category: Liu H-W]]
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[[Category: Transferase]]
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Current revision

Spinosyn Rhamnosyltransferase SpnG

PDB ID 3tsa

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