1CE7

MISTLETOE LECTIN I FROM VISCUM ALBUM

Summary for 1CE7

• Entry DOI: 10.2210/pdb1ce7/pdb
• Descriptor: PROTEIN (RIBOSOME-INACTIVATING PROTEIN TYPE II), 2-acetamido-2-deoxy-beta-D-glucopyranose, ... (4 entities in total)
• Functional Keywords: ribosome-inactivating protein type ii, ribosome
• Biological source: Viscum album (European mistletoe); More
• Total number of polymer chains: 2
• Total formula weight: 53473.56

Authors

Krauspenhaar, R.,Eschenburg, S.,Perbandt, M.,Kornilov, V.,Konareva, N.,Mikailova, I.,Stoeva, S.,Wacker, R.,Maier, T.,Singh, T.P.,Mikhailov, A.,Voelter, W.,Betzel, C. (deposition date: 1999-03-18, release date: 2000-03-20, Last modification date: 2023-08-09)

Primary citation

Krauspenhaar, R.,Eschenburg, S.,Perbandt, M.,Kornilov, V.,Konareva, N.,Mikailova, I.,Stoeva, S.,Wacker, R.,Maier, T.,Singh, T.P.,Mikhailov, A.,Voelter, W.,Betzel, C.
Crystal structure of mistletoe lectin I from Viscum album.
Biochem.Biophys.Res.Commun., 257:418-424, 1999

PubMed Abstract: The crystal structure of the ribosome-inactivating protein (RIP) mistletoe lectin I (ML-I) from Viscum album has been solved by molecular replacement techniques. The structure has been refined to a crystallographic R-factor of 24.5% using X-ray diffraction data to 2.8 A resolution. The heterodimeric 63-kDa protein consists of a toxic A subunit which exhibits RNA-glycosidase activity and a galactose-specific lectin B subunit. The overall protein fold is similar to that of ricin from Ricinus communis; however, unlike ricin, ML-I is already medically applied as a component of a commercially available misteltoe extract with immunostimulating potency and for the treatment of human cancer. The three-dimensional structure reported here revealed structural details of this pharmaceutically important protein. The comparison to the structure of ricin gives more insights into the functional mechanism of this protein, provides structural details for further protein engineering studies, and may lead to the development of more effective therapeutic RIPs.

PubMed: 10198229
DOI: 10.1006/bbrc.1999.0470

Experimental method

X-RAY DIFFRACTION (2.7 Å)