7xpr: Difference between revisions
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==Crystal structrue of SeMet-MtdL:GDP== | |||
<StructureSection load='7xpr' size='340' side='right'caption='[[7xpr]], [[Resolution|resolution]] 2.10Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[7xpr]] 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=7XPR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7XPR 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]] 2.1Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GDP:GUANOSINE-5-DIPHOSPHATE'>GDP</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</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=7xpr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7xpr OCA], [https://pdbe.org/7xpr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7xpr RCSB], [https://www.ebi.ac.uk/pdbsum/7xpr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7xpr ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/G8HX37_9ACTN G8HX37_9ACTN] | |||
<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®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
<div class="pdbe-citations 7xpr" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Marinactinospora thermotolerans]] | |||
[[Category: He C]] | |||
[[Category: Li FD]] | |||
Latest revision as of 17:13, 6 November 2024
Crystal structrue of SeMet-MtdL:GDPCrystal structrue of SeMet-MtdL:GDP
Structural highlights
FunctionPublication Abstract from PubMedMembers 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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