3GWJ
Crystal structure of Antheraea pernyi arylphorin
3GWJ の概要
| エントリーDOI | 10.2210/pdb3gwj/pdb |
| 関連するPDBエントリー | 1HCY |
| 分子名称 | Arylphorin, alpha-D-glucopyranose-(1-3)-alpha-D-mannopyranose-(1-2)-alpha-D-mannopyranose-(1-2)-alpha-D-mannopyranose-(1-3)-[alpha-D-mannopyranose-(1-2)-alpha-D-mannopyranose-(1-3)-[alpha-D-mannopyranose-(1-2)-alpha-D-mannopyranose-(1-6)]alpha-D-mannopyranose-(1-6)]beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, ... (5 entities in total) |
| 機能のキーワード | arylphorin, mono-glucosylated n-glycan, stability, glycosylation, glycoprotein, secreted, storage protein, oxygen transport |
| 由来する生物種 | Antheraea pernyi (Chinese oak silk moth) |
| 細胞内の位置 | Secreted, extracellular space (By similarity): Q7Z1F8 |
| タンパク質・核酸の鎖数 | 6 |
| 化学式量合計 | 498111.52 |
| 構造登録者 | |
| 主引用文献 | Ryu, K.S.,Lee, J.O.,Kwon, T.H.,Choi, H.H.,Park, H.S.,Hwang, S.K.,Lee, Z.W.,Lee, K.B.,Han, Y.H.,Choi, Y.S.,Jeon, Y.H.,Cheong, C.,Kim, S. The presence of monoglucosylated N196-glycan is important for the structural stability of storage protein, arylphorin Biochem.J., 421:87-96, 2009 Cited by PubMed 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. PubMed: 19358695DOI: 10.1042/BJ20082170 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (2.43 Å) |
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