1m2t
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Mistletoe Lectin I from Viscum album in Complex with Adenine Monophosphate. Crystal Structure at 1.9 A Resolution
OverviewOverview
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.
About this StructureAbout this Structure
1M2T is a Protein complex structure of sequences from Viscum album with NAG, FUC, ADE and GOL as ligands. Active as rRNA N-glycosylase, with EC number 3.2.2.22 Full crystallographic information is available from OCA.
ReferenceReference
Crystallisation under microgravity of mistletoe lectin I from Viscum album with adenine monophosphate and the crystal structure at 1.9 A resolution., Krauspenhaar R, Rypniewski W, Kalkura N, Moore K, DeLucas L, Stoeva S, Mikhailov A, Voelter W, Betzel Ch, Acta Crystallogr D Biol Crystallogr. 2002 Oct;58(Pt 10 Pt 1):1704-7. Epub, 2002 Sep 26. PMID:12351890
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