7s69
From Proteopedia
(Difference between revisions)
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<StructureSection load='7s69' size='340' side='right'caption='[[7s69]], [[Resolution|resolution]] 3.04Å' scene=''> | <StructureSection load='7s69' size='340' side='right'caption='[[7s69]], [[Resolution|resolution]] 3.04Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'> | + | <table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7S69 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7S69 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]] 3.04Å</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]] 3.04Å</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=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></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=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</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=7s69 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7s69 OCA], [https://pdbe.org/7s69 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7s69 RCSB], [https://www.ebi.ac.uk/pdbsum/7s69 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7s69 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=7s69 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7s69 OCA], [https://pdbe.org/7s69 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7s69 RCSB], [https://www.ebi.ac.uk/pdbsum/7s69 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7s69 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
| - | == Function == | ||
| - | [https://www.uniprot.org/uniprot/Q561K8_XENLA Q561K8_XENLA] | ||
| - | <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 7s69" style="background-color:#fffaf0;"></div> | ||
==See Also== | ==See Also== | ||
*[[Phosphotransferase 3D structures|Phosphotransferase 3D structures]] | *[[Phosphotransferase 3D structures|Phosphotransferase 3D structures]] | ||
| - | == References == | ||
| - | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| - | [[Category: Xenopus laevis]] | ||
[[Category: Gorelik A]] | [[Category: Gorelik A]] | ||
[[Category: Illes K]] | [[Category: Illes K]] | ||
[[Category: Nagar B]] | [[Category: Nagar B]] | ||
Current revision
N-acetylglucosamine-1-phosphotransferase (GNPT) gamma subunit (GNPTG), from clawed frog
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