4END

Crystal structure of anti-HIV actinohivin in complex with alpha-1,2-mannobiose (P 2 21 21 form)

4END の概要

• エントリーDOI: 10.2210/pdb4end/pdb
• 関連するPDBエントリー: 3A07 4DEN
• 関連するBIRD辞書のPRD_ID: PRD_900111
• 分子名称: Actinohivin, alpha-D-mannopyranose-(1-2)-alpha-D-mannopyranose, ACETONITRILE, ... (4 entities in total)
• 機能のキーワード: actinohivin, anti-hiv lectin, high-mannose type glycan, antiviral protein
• 由来する生物種: Actinomycete sp.
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 13641.49

構造登録者

Hoque, M.M.,Suzuki, K.,Tsunoda, M.,Jiang, J.,Zhang, F.,Takahashi, A.,Naomi, O.,Zhang, X.,Sekiguchi, T.,Tanaka, H.,Omura, S.,Takenaka, A. (登録日: 2012-04-13, 公開日: 2013-07-17, 最終更新日: 2025-08-06)

主引用文献

Suzuki, K.,Tsunoda, M.,Hoque, M.M.,Zhang, F.,Jiang, J.,Zhang, X.,Ohbayashi, N.,Tanaka, H.,Takenaka, A.
Peculiarity in crystal packing of anti-HIV lectin actinohivin in complex with alpha (1-2)mannobiose.
Acta Crystallogr.,Sect.D, 69:1818-1825, 2013

PubMed Abstract: Previously, the anti-HIV lectin actinohivin (AH) was cocrystallized with the target α(1-2)mannobiose (MB) in the apparent space group P213. However, three MB-bound AH rotamers generated by ±120° rotations around the molecular pseudo-threefold rotation axis are packed randomly in the unit cell according to P212121 symmetry [Hoque et al. (2012). Acta Cryst. D68, 1671-1679]. It was found that the AH used for crystallization contains short peptides attached to the N-terminus [Suzuki et al. (2012). Acta Cryst. F68, 1060-1063], which cause packing disorder. In the present study, the fully mature homogeneous AH has been cocrystallized with MB into two new crystal forms at different pH. X-ray analyses of the two forms reveal that they have peculiar character in that the space groups are the same, P22121, and the unit-cell parameters are almost the same with the exception of the length of the a axis, which is doubled in one form. The use of homogeneous AH resulted in the absence of disorder in both crystals and an improvement in the resolution, thereby establishing the basis for AH binding to the target MB. In addition, the two crystal structures clarify the interaction modes between AH molecules, which is important knowledge for understanding the multiple binding effect generated when two AH molecules are linked together with a short peptide [Takahashi et al. (2011). J. Antibiot. 64, 551-557].

PubMed: 23999305
DOI: 10.1107/S0907444913017812

実験手法

X-RAY DIFFRACTION (1.9 Å)