8jl1

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== Disease ==
== Disease ==
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[https://www.uniprot.org/uniprot/HGNAT_HUMAN HGNAT_HUMAN] Sanfilippo syndrome type C;Retinitis pigmentosa. The disease is caused by variants affecting the gene represented in this entry. The disease is caused by variants affecting the gene represented in this entry.
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[https://www.uniprot.org/uniprot/HGNAT_HUMAN HGNAT_HUMAN] Retinitis pigmentosa;Sanfilippo syndrome type C. The disease is caused by variants affecting the gene represented in this entry. The disease is caused by variants affecting the gene represented in this entry.
== Function ==
== Function ==
[https://www.uniprot.org/uniprot/HGNAT_HUMAN HGNAT_HUMAN] Lysosomal acetyltransferase that acetylates the non-reducing terminal alpha-glucosamine residue of intralysosomal heparin or heparan sulfate, converting it into a substrate for luminal alpha-N-acetyl glucosaminidase.<ref>PMID:16960811</ref> <ref>PMID:17033958</ref> <ref>PMID:19823584</ref> <ref>PMID:20650889</ref>
[https://www.uniprot.org/uniprot/HGNAT_HUMAN HGNAT_HUMAN] Lysosomal acetyltransferase that acetylates the non-reducing terminal alpha-glucosamine residue of intralysosomal heparin or heparan sulfate, converting it into a substrate for luminal alpha-N-acetyl glucosaminidase.<ref>PMID:16960811</ref> <ref>PMID:17033958</ref> <ref>PMID:19823584</ref> <ref>PMID:20650889</ref>
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== Publication Abstract from PubMed ==
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Lysosomal transmembrane acetylation of heparan sulfates (HS) is catalyzed by HS acetyl-CoA:alpha-glucosaminide N-acetyltransferase (HGSNAT), whose dysfunction leads to lysosomal storage diseases. The mechanism by which HGSNAT, the sole non-hydrolase enzyme in HS degradation, brings cytosolic acetyl-coenzyme A (Ac-CoA) and lysosomal HS together for N-acyltransferase reactions remains unclear. Here, we present cryogenic-electron microscopy structures of HGSNAT alone, complexed with Ac-CoA and with acetylated products. These structures explain that Ac-CoA binding from the cytosolic side causes dimeric HGSNAT to form a transmembrane tunnel. Within this tunnel, catalytic histidine and asparagine approach the lumen and instigate the transfer of the acetyl group from Ac-CoA to the glucosamine group of HS. Our study unveils a transmembrane acetylation mechanism that may help advance therapeutic strategies targeting lysosomal storage diseases.
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Structure and mechanism of lysosome transmembrane acetylation by HGSNAT.,Xu R, Ning Y, Ren F, Gu C, Zhu Z, Pan X, Pshezhetsky AV, Ge J, Yu J Nat Struct Mol Biol. 2024 Oct;31(10):1502-1508. doi: 10.1038/s41594-024-01315-5. , Epub 2024 May 20. PMID:38769387<ref>PMID:38769387</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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== References ==
== References ==
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membrane proteins

PDB ID 8jl1

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