7xpv: Difference between revisions
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[7xpv]] 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=7XPV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7XPV FirstGlance]. <br> | <table><tr><td colspan='2'>[[7xpv]] 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=7XPV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7XPV FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GRJ:[[(2~{R},3~{S},4~{R},5~{R})-5-(2-azanyl-6-oxidanyl-purin-9-yl)-3,4-bis(oxidanyl)oxolan-2-yl]methoxy-oxidanyl-phosphoryl]+[(2~{S},3~{S},4~{S},5~{R})-3,4-bis(oxidanyl)-5-[(1~{S})-1-oxidanylethyl]oxolan-2-yl]+hydrogen+phosphate'>GRJ</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene></td></tr> | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.4Å</td></tr> | ||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GRJ:[[(2~{R},3~{S},4~{R},5~{R})-5-(2-azanyl-6-oxidanyl-purin-9-yl)-3,4-bis(oxidanyl)oxolan-2-yl]methoxy-oxidanyl-phosphoryl]+[(2~{S},3~{S},4~{S},5~{R})-3,4-bis(oxidanyl)-5-[(1~{S})-1-oxidanylethyl]oxolan-2-yl]+hydrogen+phosphate'>GRJ</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=7xpv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7xpv OCA], [https://pdbe.org/7xpv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7xpv RCSB], [https://www.ebi.ac.uk/pdbsum/7xpv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7xpv 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=7xpv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7xpv OCA], [https://pdbe.org/7xpv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7xpv RCSB], [https://www.ebi.ac.uk/pdbsum/7xpv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7xpv ProSAT]</span></td></tr> | ||
</table> | </table> | ||
Latest revision as of 20:57, 29 November 2023
crysteal structure of MtdL-S228A-His soaked with GDP-Fucf and Mncrysteal structure of MtdL-S228A-His soaked with GDP-Fucf and Mn
Structural highlights
Publication 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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