8xj4
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==Structure of prostatic acid phosphatase in human semen== | |
| + | <StructureSection load='8xj4' size='340' side='right'caption='[[8xj4]], [[Resolution|resolution]] 3.19Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[8xj4]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8XJ4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8XJ4 FirstGlance]. <br> | ||
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 3.19Å</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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=8xj4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8xj4 OCA], [https://pdbe.org/8xj4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8xj4 RCSB], [https://www.ebi.ac.uk/pdbsum/8xj4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8xj4 ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/PPAP_HUMAN PPAP_HUMAN] A non-specific tyrosine phosphatase that dephosphorylates a diverse number of substrates under acidic conditions (pH 4-6) including alkyl, aryl, and acyl orthophosphate monoesters and phosphorylated proteins. Has lipid phosphatase activity and inactivates lysophosphatidic acid in seminal plasma.<ref>PMID:15280042</ref> <ref>PMID:18083097</ref> <ref>PMID:19403677</ref> <ref>PMID:20498373</ref> Isoform 2: the cellular form also has ecto-5'-nucleotidase activity in dorsal root ganglion (DRG) neurons. Generates adenosine from AMP which acts as a pain suppressor. Acts as a tumor suppressor of prostate cancer through dephosphorylation of ERBB2 and deactivation of MAPK-mediated signaling.<ref>PMID:15280042</ref> <ref>PMID:18083097</ref> <ref>PMID:19403677</ref> <ref>PMID:20498373</ref> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Prostatic acid phosphatase (PAP) is a glycoprotein that plays a crucial role in the hydrolysis of phosphate ester present in prostatic exudates. It is a well-established indicator for prostate cancer due to its elevated serum levels in disease progression. Despite its abundance in semen, PAP's influence on male fertility has not been extensively studied. In our study, we report a significantly optimized method for purifying human endogenous PAP, achieving remarkably high efficiency and active protein recovery rate. This achievement allowed us to better analyze and understand the PAP protein. We determined the cryo-electron microscopic (Cryo-EM) structure of prostatic acid phosphatase in its physiological state for the first time. Our structural and gel filtration analysis confirmed the formation of a tight homodimer structure of human PAP. This functional homodimer displayed an elongated conformation in the cryo-EM structure compared to the previously reported crystal structure. Additionally, there was a notable 5-degree rotation in the angle between the alpha domain and alpha/beta domain of each monomer. Through structural analysis, we revealed three potential glycosylation sites: Asn94, Asn220, and Asn333. These sites contained varying numbers and forms of glycosyl units, suggesting sugar moieties influence PAP function. Furthermore, we found that the active sites of PAP, His44 and Asp290, are located between the two protein domains. Overall, our study not only provide an optimized approach for PAP purification, but also offer crucial insights into its structural characteristics. These findings lay the groundwork for further investigations into the physiological function and potential therapeutic applications of this important protein. | ||
| - | + | Purification, identification and Cryo-EM structure of prostatic acid phosphatase in human semen.,Liu X, Yu L, Xia Z, Li J, Meng W, Min L, Li F, Wang X Biochem Biophys Res Commun. 2024 Apr 2;702:149652. doi: , 10.1016/j.bbrc.2024.149652. Epub 2024 Feb 7. PMID:38341922<ref>PMID:38341922</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| + | <div class="pdbe-citations 8xj4" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Homo sapiens]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Deng D]] | ||
| + | [[Category: Li JL]] | ||
| + | [[Category: Liu XZ]] | ||
| + | [[Category: Wang X]] | ||
Current revision
Structure of prostatic acid phosphatase in human semen
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Categories: Homo sapiens | Large Structures | Deng D | Li JL | Liu XZ | Wang X
