1M2T

Mistletoe Lectin I from Viscum album in Complex with Adenine Monophosphate. Crystal Structure at 1.9 A Resolution

1M2T の概要

• エントリーDOI: 10.2210/pdb1m2t/pdb
• 関連するPDBエントリー: 2MLL
• 分子名称: mistletoe lectin I A chain, mistletoe lectin I B chain, 2-acetamido-2-deoxy-beta-D-glucopyranose, ... (7 entities in total)
• 機能のキーワード: ribosome inactivation, ribosome inhibitor, hydrolase
• 由来する生物種: Viscum album (European mistletoe); 詳細
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 58916.44

構造登録者

Krauspenhaar, R.,Rypniewski, W.,Kalkura, N.,Moore, K.,DeLucas, L.,Stoeva, S.,Mikhailov, A.,Voelter, W.,Betzel, C. (登録日: 2002-06-25, 公開日: 2003-06-24, 最終更新日: 2024-11-20)

主引用文献

Krauspenhaar, R.,Rypniewski, W.,Kalkura, N.,Moore, K.,DeLucas, L.,Stoeva, S.,Mikhailov, A.,Voelter, W.,Betzel, C.h.
Crystallisation under microgravity of mistletoe lectin I from Viscum album with adenine monophosphate and the crystal structure at 1.9 A resolution.
Acta Crystallogr.,Sect.D, 58:1704-1707, 2002

PubMed Abstract: The crystal structure of the ribosome-inactivating protein (RIP) mistletoe lectin I (ML-I) from Viscum album in complex with adenine has been refined to 1.9 A resolution. High quality crystals of the ML-I complex were obtained by the method of vapour diffusion using the high density protein crystal growth system (HDPCG) on the international space station, mission ISS 6A. Hexagonal crystals were grown during three months under microgravity conditions. Diffraction data to 1.9A were collected applying synchrotron radiation and cryo- techniques. The structure was refined subsequently to analyse the structure of ML-I and particularly the active site conformation, complexed by adenine that mimics the RNA substrate binding.

PubMed: 12351890
DOI: 10.1107/S0907444902014270

実験手法

X-RAY DIFFRACTION (1.89 Å)