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TitlePurification, identification and Cryo-EM structure of prostatic acid phosphatase in human semen.
Journal, issue, pagesBiochem Biophys Res Commun, Vol. 702, Page 149652, Year 2024
Publish dateApr 2, 2024
AuthorsXuanzhong Liu / Lin Yu / Zhili Xia / Jialu Li / Wenbo Meng / Ling Min / Fuping Li / Xiang Wang /
PubMed AbstractProstatic 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 ...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 α domain and α/β 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.
External linksBiochem Biophys Res Commun / PubMed:38341922
MethodsEM (single particle)
Resolution3.19 Å
Structure data

38393

8xj4

EMDB-38393, PDB-8xj4:
Structure of prostatic acid phosphatase in human semen
Method: EM (single particle) / Resolution: 3.19 Å

Chemicals

ChemComp-NAG:
2-acetamido-2-deoxy-beta-D-glucopyranose

ChemComp-MAN:
alpha-D-mannopyranose

Source
  • homo sapiens (human)
KeywordsCELL CYCLE / Acid phosphatase

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