1ORL

1H NMR structure determination of Viscotoxin C1

Summary for 1ORL

• Entry DOI: 10.2210/pdb1orl/pdb
• Related: 1ED0
• NMR Information: BMRB: 5767
• Descriptor: Viscotoxin C1 (1 entity in total)
• Functional Keywords: helix-turn-helix, beta-sheet, concentric motif of disulphide bridges, toxin
• Biological source: Viscum album (European mistletoe)
• Cellular location: Secreted: P08943
• Total number of polymer chains: 1
• Total formula weight: 4954.69

Authors

Molinari, H.,Romagnoli, S.,Fogolari, F.,Catalano, M.,Urech, K.,Giannattasio, M.,Ragona, L. (deposition date: 2003-03-14, release date: 2003-04-01, Last modification date: 2024-10-16)

Primary citation

Romagnoli, S.,Fogolari, F.,Catalano, M.,Zetta, L.,Schaller, G.,Urech, K.,Giannattasio, M.,Ragona, L.,Molinari, H.
NMR solution structure of viscotoxin C1 from Viscum album species Coloratum ohwi: toward a structure-function analysis of viscotoxins.
Biochemistry, 42:12503-12510, 2003

PubMed Abstract: The high resolution three-dimensional structure of the newly discovered plant viscotoxin C1, from the Asiatic Viscum album ssp. Coloratum ohwi, has been determined in solution by (1)H NMR spectroscopy at pH 3.6 and 285 K. The viscotoxin C1-fold, consisting of a helix-turn-helix motif and a short stretch of an antiparralel beta-sheet is very similar to that found for the highly similar viscotoxins A2 and A3 and for other related thionins. Different functional properties of members of the thionin family are discussed here in light of the structural and electrostatic properties. Among the very homologous family of alpha- and beta-thionins, known for their antimicrobial activity, the viscotoxin subfamily differs from the other members because of its high toxicity against tumoral cells. Key residues for the modulation of viscotoxin cytotoxicity have been identified on the basis of sequence and structural alignment.

PubMed: 14580196
DOI: 10.1021/bi034762t

Experimental method

SOLUTION NMR