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3tsa
From Proteopedia
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| - | [[ | + | ==Spinosyn Rhamnosyltransferase SpnG== |
| + | <StructureSection load='3tsa' size='340' side='right' caption='[[3tsa]], [[Resolution|resolution]] 1.70Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[3tsa]] is a 2 chain structure with sequence from [http://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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3TSA FirstGlance]. <br> | ||
| + | </td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GLC:ALPHA-D-GLUCOSE'>GLC</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene><br> | ||
| + | <tr><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">spnG ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=60894 Saccharopolyspora spinosa])</td></tr> | ||
| + | <tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3tsa FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3tsa OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3tsa RCSB], [http://www.ebi.ac.uk/pdbsum/3tsa PDBsum]</span></td></tr> | ||
| + | <table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | 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 >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. | ||
| - | + | 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®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | == References == | |
| - | + | <references/> | |
| - | + | __TOC__ | |
| - | + | </StructureSection> | |
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[[Category: Saccharopolyspora spinosa]] | [[Category: Saccharopolyspora spinosa]] | ||
[[Category: Isiorho, E A.]] | [[Category: Isiorho, E A.]] | ||
Revision as of 06:18, 5 June 2014
Spinosyn Rhamnosyltransferase SpnG
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