Proton NMR studies of apo-neocarzinostatin from Streptomyces carzinostaticus. Sequence-specific assignment and secondary structure.
The sequence-specific resonance assignment of apo-neocarzinostatin from Streptomyces carzinostaticus was carried out from two-dimensional proton-NMR spectra. The assignments were obtained for the backbone protons of 111 of the 113 residues of the protein, missing the two C alpha H of one glycine but including 3 of the 4 prolines. The majority of side chain protons were also assigned. The secondary structure derived from the analysis of sequential connections corresponds to ten beta-strands separated by clearly identified loops and turns. Inter-strand connectivities and slowly exchanging amide protons confirm the presence of the two disulfide bridges from Cys37 to Cys47 and from Cys88 to Cys93 and indicate a global folding similar to that of the similar proteins, actinoxanthin and macromomycin, for which crystallographic data are available.
Adjadj
E
E
U 219 INSERM, Institut Curie, Biologie, Centre Universitaire, Orsay, France.
Mispelter
J
J
Quiniou
E
E
Dimicoli
J L
JL
Favaudon
V
V
Lhoste
J M
JM
D000409:Alanine; D000595:Amino Acid Sequence; D000596:Amino Acids / Q000032:analysis; D000903:Antibiotics, Antineoplastic / Q000302:isolation & purification*; D005998:Glycine; D007930:Leucine; D009682:Magnetic Resonance Spectroscopy / Q000379:methods; D008969:Molecular Sequence Data; D011487:Protein Conformation; D012996:Solutions; D013302:Streptomyces / Q000032:analysis*; D013912:Threonine; D014633:Valine; D009353:Zinostatin / Q000302:isolation & purification*
D000596:Amino Acids; D000903:Antibiotics, Antineoplastic; D012996:Solutions; D013912:Threonine; D009353:Zinostatin; D007930:Leucine; D014633:Valine; D000409:Alanine; D005998:Glycine