1M2T

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

Summary for 1M2T

• Entry DOI: 10.2210/pdb1m2t/pdb
• Related: 2MLL
• Descriptor: mistletoe lectin I A chain, mistletoe lectin I B chain, 2-acetamido-2-deoxy-beta-D-glucopyranose, ... (7 entities in total)
• Functional Keywords: ribosome inactivation, ribosome inhibitor, hydrolase
• Biological source: Viscum album (European mistletoe); More
• Total number of polymer chains: 2
• Total formula weight: 58916.44

Authors

Krauspenhaar, R.,Rypniewski, W.,Kalkura, N.,Moore, K.,DeLucas, L.,Stoeva, S.,Mikhailov, A.,Voelter, W.,Betzel, C. (deposition date: 2002-06-25, release date: 2003-06-24, Last modification date: 2024-11-20)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (1.89 Å)