The presence of monoglucosylated N196-glycan is important for the structural stability of storage protein, arylphorin = 저장단백질 arylphorin의 구조안정성을 위해 중요한 monoglucosylated N196-glycan

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Title
The presence of monoglucosylated N196-glycan is important for the structural stability of storage protein, arylphorin = 저장단백질 arylphorin의 구조안정성을 위해 중요한 monoglucosylated N196-glycan
Author(s)
K S Ryu; J O Lee; T H Kwon; Han Ho Choi; Hong-Seog Park; S K Hwang; Z W Lee; K B Lee; Y H Han; Y S Choi; Y H Jeon; C Cheong; S Kim
Bibliographic Citation
Biochemical Journal, vol. 421, no. 1, pp. 87-96
Publication Year
2009
Abstract
Although N-glycosylation has been known to increase the stability of glycoproteins, it is difficult to assess the structural importance of glycans in the stabilization of glycoproteins. APA (Antheraea pernyi arylphorin) is an insect hexamerin that has two N-glycosylations at Asn196 and Asn344 respectively. The glycosylation of Asn344 is critical for the folding process; however, glycosylation of Asn196 is not. Interestingly, the N196-glycan (glycosylation of Asn196) remains in an immature form (Glc1Man9GlcNAc2). The mutation of Asn196 to glutamine does not change the ecdysone-binding activity relative to that of the wild-type. In the present study,we determined the crystal structure of APA, and all sugar moieties of the N196-glycan were clearly observed in the electron-density map. Although the sugar moieties of the glycan generally have high structural flexibility, most sugar moieties of the N196-glycan were well organized in the deep cleft of the subunit interface and mediated many inter- and intrasubunit hydrogen bonds. Analytical ultracentrifugation and GdmCl (guanidinium chloride) unfolding experiments revealed that the presence of the N196-glycan was important for stabilizing the hexameric state and overall stability of APA respectively. Our results could provide a structural basis for studying not only other glycoproteins that carry an immature N-glycan, but also the structural role of N-glycans that are located in the deep cleft of a protein.
Keyword
arylphorinecdysoneglycosylationprotein stabilityprotein structureX-ray crystallography
ISSN
0264-6021
Publisher
Portland Press Ltd
DOI
http://dx.doi.org/10.1042/BJ20082170
Type
Article
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1. Journal Articles > Journal Articles
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