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==N-acetylglucosamine-1-phosphotransferase (GNPT) alpha and beta subunits (GNPTAB) catalytic domain, from zebrafish, in complex with uridine diphosphate N-acetylglucosamine (UDP-GlcNAc) and magnesium== | ==N-acetylglucosamine-1-phosphotransferase (GNPT) alpha and beta subunits (GNPTAB) catalytic domain, from zebrafish, in complex with uridine diphosphate N-acetylglucosamine (UDP-GlcNAc) and magnesium== | ||
<StructureSection load='7sj2' size='340' side='right'caption='[[7sj2]]' scene=''> | <StructureSection load='7sj2' size='340' side='right'caption='[[7sj2]], [[Resolution|resolution]] 2.30Å' 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=7SJ2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7SJ2 FirstGlance]. <br> | <table><tr><td colspan='2'>[[7sj2]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7SJ2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7SJ2 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=7sj2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7sj2 OCA], [https://pdbe.org/7sj2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7sj2 RCSB], [https://www.ebi.ac.uk/pdbsum/7sj2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7sj2 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=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=UD1:URIDINE-DIPHOSPHATE-N-ACETYLGLUCOSAMINE'>UD1</scene>, <scene name='pdbligand=FUC:ALPHA-L-FUCOSE'>FUC</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</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=7sj2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7sj2 OCA], [https://pdbe.org/7sj2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7sj2 RCSB], [https://www.ebi.ac.uk/pdbsum/7sj2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7sj2 ProSAT]</span></td></tr> | |||
</table> | </table> | ||
== Function == | |||
[[https://www.uniprot.org/uniprot/GNPTA_DANRE GNPTA_DANRE]] Catalyzes the formation of mannose 6-phosphate (M6P) markers on high mannose type oligosaccharides in the Golgi apparatus. M6P residues are required to bind to the M6P receptors (MPR), which mediate the vesicular transport of lysosomal enzymes to the endosomal/prelysosomal compartment.[UniProtKB:Q3T906] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The mannose-6-phosphate (M6P) pathway is responsible for the transport of hydrolytic enzymes to lysosomes. N-acetylglucosamine-1-phosphotransferase (GNPT) catalyzes the first step of tagging these hydrolases with M6P, which when recognized by receptors in the Golgi diverts them to lysosomes. Genetic defects in the GNPT subunits, GNPTAB and GNPTG, cause the lysosomal storage diseases mucolipidosis types II and III. To better understand its function, we determined partial three-dimensional structures of the GNPT complex. The catalytic domain contains a deep cavity for binding of uridine diphosphate-N-acetylglucosamine, and the surrounding residues point to a one-step transfer mechanism. An isolated structure of the gamma subunit of GNPT reveals that it can bind to mannose-containing glycans in different configurations, suggesting that it may play a role in directing glycans into the active site. These findings may facilitate the development of therapies for lysosomal storage diseases. | |||
Structures of the mannose-6-phosphate pathway enzyme, GlcNAc-1-phosphotransferase.,Gorelik A, Illes K, Bui KH, Nagar B Proc Natl Acad Sci U S A. 2022 Aug 16;119(33):e2203518119. doi:, 10.1073/pnas.2203518119. Epub 2022 Aug 8. PMID:35939698<ref>PMID:35939698</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 7sj2" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Gorelik A]] | [[Category: Gorelik, A]] | ||
[[Category: Illes K]] | [[Category: Illes, K]] | ||
[[Category: Nagar B]] | [[Category: Nagar, B]] | ||
[[Category: Gnpt]] | |||
[[Category: Lysosome]] | |||
[[Category: Mannose 6-phosphate]] | |||
[[Category: Mucolipidosis]] | |||
[[Category: Transferase]] | |||