Related ArticlesProton NMR studies of apo-neocarzinostatin from Streptomyces carzinostaticus. Sequence-specific assignment and secondary structure.
Eur J Biochem. 1990 Jun 20;190(2):263-71
Authors: Adjadj E, Mispelter J, Quiniou E, Dimicoli JL, Favaudon V, Lhoste JM
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.
[NMR paper] Solution NMR structure investigation for releasing mechanism of neocarzinostatin chro
Solution NMR structure investigation for releasing mechanism of neocarzinostatin chromophore from the holoprotein.
Related Articles Solution NMR structure investigation for releasing mechanism of neocarzinostatin chromophore from the holoprotein.
J Biol Chem. 2005 Mar 25;280(12):11340-6
Authors: Takashima H, Yoshida T, Ishino T, Hasuda K, Ohkubo T, Kobayashi Y
Holo-neocarzinostatin (holo-NCS) is a complex protein carrying the anti-tumor active enediyne ring chromophore by a scaffold consisting of an immunoglobulin-like seven-stranded...
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[NMR paper] NMR structure of the Streptomyces metalloproteinase inhibitor, SMPI, isolated from St
NMR structure of the Streptomyces metalloproteinase inhibitor, SMPI, isolated from Streptomyces nigrescens TK-23: another example of an ancestral beta gamma-crystallin precursor structure.
Related Articles NMR structure of the Streptomyces metalloproteinase inhibitor, SMPI, isolated from Streptomyces nigrescens TK-23: another example of an ancestral beta gamma-crystallin precursor structure.
J Mol Biol. 1998 Sep 18;282(2):421-33
Authors: Ohno A, Tate S, Seeram SS, Hiraga K, Swindells MB, Oda K, Kainosho M
The Streptomyces metalloproteinase...
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[NMR paper] Internal motions of apo-neocarzinostatin as studied by 13C NMR methine relaxation at
Internal motions of apo-neocarzinostatin as studied by 13C NMR methine relaxation at natural abundance.
Related Articles Internal motions of apo-neocarzinostatin as studied by 13C NMR methine relaxation at natural abundance.
J Biomol NMR. 1995 Apr;5(3):233-44
Authors: Mispelter J, Lefèvre C, Adjadj E, Quiniou E, Favaudon V
Dynamics of the backbone and some side chains of apo-neocarzinostatin, a 10.7 kDa carrier protein, have been studied from 13C relaxation rates R1, R2 and steady-state 13C-(1H) NOEs, measured at natural abundance. Relaxation...
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[NMR paper] Assignment of the protonated 13C resonances of apo-neocarzinostatin by 2D heteronucle
Assignment of the protonated 13C resonances of apo-neocarzinostatin by 2D heteronuclear NMR spectroscopy at natural abundance.
Related Articles Assignment of the protonated 13C resonances of apo-neocarzinostatin by 2D heteronuclear NMR spectroscopy at natural abundance.
J Biomol NMR. 1994 Sep;4(5):689-702
Authors: Lefevre C, Adjadj E, Quiniou E, Mispelter J
Nearly complete assignment of the protonated carbon resonances of apo-neocarzinostatin, a 113-amino acid antitumor antibiotic carrier protein, has been achieved at natural 13C abundance...
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[NMR paper] Three-dimensional solution structure of apo-neocarzinostatin from Streptomyces carzin
Three-dimensional solution structure of apo-neocarzinostatin from Streptomyces carzinostaticus determined by NMR spectroscopy.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www3.interscience.wiley.com-aboutus-images-wiley_interscience_pubmed_logo_FREE_120x27.gif Related Articles Three-dimensional solution structure of apo-neocarzinostatin from Streptomyces carzinostaticus determined by NMR spectroscopy.
Eur J Biochem. 1992 Feb 1;203(3):505-11
Authors: Adjadj E, Quiniou E, Mispelter J, Favaudon V, Lhoste JM
The three-dimensional...
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[NMR paper] Reductive cleavage and regeneration of the disulfide bonds in Streptomyces subtilisin
Reductive cleavage and regeneration of the disulfide bonds in Streptomyces subtilisin inhibitor (SSI) as studied by the carbonyl 13C NMR resonances of cysteinyl residues.
Related Articles Reductive cleavage and regeneration of the disulfide bonds in Streptomyces subtilisin inhibitor (SSI) as studied by the carbonyl 13C NMR resonances of cysteinyl residues.
J Biomol NMR. 1991 May;1(1):49-64
Authors: Uchida K, Miyake Y, Kainosho M
Four enhanced carbonyl carbon resonances were observed when Streptomyces subtilisin inhibitor (SSI) was labeled by...
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[NMR paper] Two- and three-dimensional proton NMR studies of apo-neocarzinostatin.
Two- and three-dimensional proton NMR studies of apo-neocarzinostatin.
Related Articles Two- and three-dimensional proton NMR studies of apo-neocarzinostatin.
Biochemistry. 1991 Aug 6;30(31):7730-9
Authors: Gao XL, Burkhart W
Neocarzinostatin (NCS) is an antitumor protein from Streptomyces carzinostaticus that is identical in apo-protein sequence with mitomalcin (MMC) from Streptomyces malayensis. We describe the use of apo-NCS as a model system for applying combined two- and three-dimensional (2D and 3D) proton NMR spectroscopy to the...
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[NMR paper] Two- and three-dimensional proton NMR studies of apo-neocarzinostatin.
Two- and three-dimensional proton NMR studies of apo-neocarzinostatin.
Related Articles Two- and three-dimensional proton NMR studies of apo-neocarzinostatin.
Biochemistry. 1991 Aug 6;30(31):7730-9
Authors: Gao XL, Burkhart W
Neocarzinostatin (NCS) is an antitumor protein from Streptomyces carzinostaticus that is identical in apo-protein sequence with mitomalcin (MMC) from Streptomyces malayensis. We describe the use of apo-NCS as a model system for applying combined two- and three-dimensional (2D and 3D) proton NMR spectroscopy to the...