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7ndl
From Proteopedia
(Difference between revisions)
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==Crystal structure of human GFAT-1 S205D== | ==Crystal structure of human GFAT-1 S205D== | ||
| - | <StructureSection load='7ndl' size='340' side='right'caption='[[7ndl]]' scene=''> | + | <StructureSection load='7ndl' size='340' side='right'caption='[[7ndl]], [[Resolution|resolution]] 2.22Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7NDL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7NDL FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[7ndl]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7NDL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7NDL FirstGlance]. <br> |
| - | </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=7ndl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7ndl OCA], [https://pdbe.org/7ndl PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7ndl RCSB], [https://www.ebi.ac.uk/pdbsum/7ndl PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7ndl ProSAT]</span></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=G6Q:GLUCOSE-6-PHOSPHATE'>G6Q</scene>, <scene name='pdbligand=GLU:GLUTAMIC+ACID'>GLU</scene></td></tr> |
| + | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=SEP:PHOSPHOSERINE'>SEP</scene></td></tr> | ||
| + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[6zmj|6zmj]], [[6zmk|6zmk]]</div></td></tr> | ||
| + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">GFPT1, GFAT, GFPT ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr> | ||
| + | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Glutamine--fructose-6-phosphate_transaminase_(isomerizing) Glutamine--fructose-6-phosphate transaminase (isomerizing)], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.6.1.16 2.6.1.16] </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=7ndl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7ndl OCA], [https://pdbe.org/7ndl PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7ndl RCSB], [https://www.ebi.ac.uk/pdbsum/7ndl PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7ndl ProSAT]</span></td></tr> | ||
</table> | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | The hexosamine pathway (HP) is a key anabolic pathway whose product uridine 5'-diphospho-N-acetyl-D-glucosamine (UDP-GlcNAc) is an essential precursor for glycosylation processes in mammals. It modulates the ER stress response and HP activation extends lifespan in Caenorhabditis elegans. The highly conserved glutamine fructose-6-phosphate amidotransferase 1 (GFAT-1) is the rate-limiting HP enzyme. GFAT-1 activity is modulated by UDP-GlcNAc feedback inhibition and via phosphorylation by protein kinase A (PKA). Molecular consequences of GFAT-1 phosphorylation, however, remain poorly understood. Here, we identify the GFAT-1 R203H substitution that elevates UDP-GlcNAc levels in C. elegans. In human GFAT-1, the R203H substitution interferes with UDP-GlcNAc inhibition and with PKA-mediated Ser205 phosphorylation. Our data indicate that phosphorylation affects the interactions of the two GFAT-1 domains to control catalytic activity. Notably, Ser205 phosphorylation has two discernible effects: it lowers baseline GFAT-1 activity and abolishes UDP-GlcNAc feedback inhibition. PKA controls the HP by uncoupling the metabolic feedback loop of GFAT-1. | ||
| + | |||
| + | Protein kinase A controls the hexosamine pathway by tuning the feedback inhibition of GFAT-1.,Ruegenberg S, Mayr FAMC, Atanassov I, Baumann U, Denzel MS Nat Commun. 2021 Apr 12;12(1):2176. doi: 10.1038/s41467-021-22320-y. PMID:33846315<ref>PMID:33846315</ref> | ||
| + | |||
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 7ndl" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| + | [[Category: Human]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| - | [[Category: Baumann U]] | + | [[Category: Baumann, U]] |
| - | [[Category: Denzel | + | [[Category: Denzel, M S]] |
| - | [[Category: Ruegenberg S]] | + | [[Category: Ruegenberg, S]] |
| + | [[Category: Gfat]] | ||
| + | [[Category: Glutamine fructose-6-phosphate amidotransferase]] | ||
| + | [[Category: Ntn hydrolase]] | ||
| + | [[Category: Transferase]] | ||
Revision as of 05:36, 28 April 2021
Crystal structure of human GFAT-1 S205D
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