PMID- 10639192
OWN - NLM
STAT- MEDLINE
DCOM- 20000223
LR  - 20190915
IS  - 0270-4137 (Print)
IS  - 0270-4137 (Linking)
VI  - 42
IP  - 3
DP  - 2000 Feb 15
TI  - Crystal structure of human prostatic acid phosphatase .
PG  - 211-8
AB  - BACKGROUND: Prostatic acid phosphatase (hPAP) is a major product of the human
      prostate gland, yet its physiological substrate remains unknown. METHODS: Human
      PAP, purified from semen, was crystallized using polyethylene glycol as the
      precipitant and its crystal structure was determined using X-ray diffraction. The
      structure was refined at 3.1 A resolution to R = 16% and R(free) = 27%. RESULTS: 
      The structure of hPAP is similar to that of other known histidine phosphatases,
      and the positions of its catalytic residues are conserved. N-linked carbohydrates
      are present at each of the possible glycosylation sites. It appears that
      high-mannose chains are attached to Asn 62 and Asp 301, while complex chains are 
      at Asn 188. CONCLUSIONS: The similarity of the three-dimensional structures of
      rat PAP and human PAP indicates that the mechanistic analyses of the catalytic
      mechanism proposed for the rat enzyme should be extended to the human enzyme
      without reservations. The crystallographic data allowed the correlation of
      attachment sites of N-linked carbohydrate chains with a given carbohydrate type. 
      The carbohydrates of the protein produced in the prostate cells and in the
      baculovirus expression system appear to differ at the site of complex
      carbohydrates attachment.
CI  - Copyright 2000 Wiley-Liss, Inc.
FAU - Jakob, C G
AU  - Jakob CG
AD  - Department of Chemistry and Biochemistry, University of South Carolina, Columbia,
      South Carolina 29208, USA.
FAU - Lewinski, K
AU  - Lewinski K
FAU - Kuciel, R
AU  - Kuciel R
FAU - Ostrowski, W
AU  - Ostrowski W
FAU - Lebioda, L
AU  - Lebioda L
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PT  - Research Support, U.S. Gov't, Non-P.H.S.
PL  - United States
TA  - Prostate
JT  - The Prostate
JID - 8101368
RN  - 0 (Carbohydrates)
RN  - EC 3.1.3.2 (Acid Phosphatase)
SB  - IM
MH  - Acid Phosphatase/*chemistry/metabolism
MH  - Binding Sites
MH  - Carbohydrates/chemistry
MH  - Crystallography, X-Ray
MH  - Glycosylation
MH  - Humans
MH  - Male
MH  - Models, Molecular
MH  - Prostate/*enzymology
MH  - Protein Conformation
MH  - Protein Processing, Post-Translational
MH  - Semen/enzymology
EDAT- 2000/01/19 09:00
MHDA- 2000/02/26 09:00
CRDT- 2000/01/19 09:00
PHST- 2000/01/19 09:00 [pubmed]
PHST- 2000/02/26 09:00 [medline]
PHST- 2000/01/19 09:00 [entrez]
AID - 10.1002/(SICI)1097-0045(20000215)42:3<211::AID-PROS7>3.0.CO;2-U [pii]
AID - 10.1002/(sici)1097-0045(20000215)42:3<211::aid-pros7>3.0.co;2-u [doi]
PST - ppublish
SO  - Prostate. 2000 Feb 15;42(3):211-8. doi:
      10.1002/(sici)1097-0045(20000215)42:3<211::aid-pros7>3.0.co;2-u.