View source for 7xpt


==Crystal structrue of MtdL:GDP:Mn soaked with GDP-Glc==
<StructureSection load='7xpt' size='340' side='right'caption='[[7xpt]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[7xpt]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Marinactinospora_thermotolerans Marinactinospora thermotolerans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7XPT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7XPT FirstGlance]. <br>
</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&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GDG:GDP-ALPHA-D-GLUCOSE'>GDG</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</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=7xpt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7xpt OCA], [https://pdbe.org/7xpt PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7xpt RCSB], [https://www.ebi.ac.uk/pdbsum/7xpt PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7xpt ProSAT]</span></td></tr>
</table>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Members of glycosyltransferase family 75 (GT75) not only reversibly catalyze the autoglycosylation of a conserved arginine residue with specific NDP-sugars but also exhibit NDP-pyranose mutase activity that reversibly converts specific NDP-pyranose to NDP-furanose. The latter activity provides valuable NDP-furanosyl donors for glycosyltransferases and requires a divalent cation as a cofactor instead of FAD used by UDP-D-galactopyranose mutase. However, details of the mechanism for NDP-pyranose mutase activity are not clear. Here we report the first crystal structures of GT75 family NDP-pyranose mutases. The novel structures of GT75 member MtdL in complex with Mn(2+) and GDP, GDP-D-glucopyranose, GDP-L-fucopyranose, GDP-L-fucofuranose, respectively, combined with site-directed mutagenesis studies, reveal key residues involved in Mn(2+) coordination, substrate binding, and catalytic reactions. We also provide a possible catalytic mechanism for this unique type of NDP-pyranose mutase. Taken together, our results highlight key elements of an enzyme family important for furanose biosynthesis.

Structures of the NDP-pyranose mutase belonging to glycosyltransferase family 75 reveal residues important for Mn(2+) coordination and substrate binding.,Du X, Chu X, Liu N, Jia X, Peng H, Xiao Y, Liu L, Yu H, Li F, He C J Biol Chem. 2023 Feb;299(2):102903. doi: 10.1016/j.jbc.2023.102903. Epub 2023 , Jan 13. PMID:36642179<ref>PMID:36642179</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 7xpt" style="background-color:#fffaf0;"></div>
== References ==
<references/>
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</StructureSection>
[[Category: Large Structures]]
[[Category: Marinactinospora thermotolerans]]
[[Category: He C]]
[[Category: Li FD]]