UMR9187 / U1196 – Chemistry, Modelling and Imaging for Biology (CMIB)

Unit publications

Year of publication 1992

E Adjadj, E Quiniou, J Mispelter, V Favaudon, J M Lhoste (1992 Sep 1)

The seven-stranded beta-barrel structure of apo-neocarzinostatin as compared to the immunoglobulin domain.

Biochimie : 74 : 853-858 : DOI : 10.1016/0300-9084(92)90068-P Learn more
Summary

The three-dimensional structure of apo-NCS, as revealed by proton NMR, is based on an antiparallel seven-stranded beta-barrel. This fold is frequently encountered in protein structures, especially for immunoglobulin domains. The strands forming the barrel are joined by flexible loops of which three are implicated in the ligand binding site of these proteins. In this paper a preliminary comparison is given with respect to the static and dynamic properties of both the constant beta-barrel and the active loops for apo-NCS and the variable VH domain of an immunoglobulin Fab’ fragment.

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Adjadj Elisabeth, Quiniou Eric, Mispelter Joël, Favaudon Vincent, Lhoste Jean-Marc (1992 Feb 1)

Three-dimensional solution structure of apo-neocarzinostatin from Streptomyces carzinostaticus determined by NMR spectroscopy.

European journal of biochemistry : 203 : 505-511 : DOI : 10.1111/j.1432-1033.1992.tb16576.x Learn more
Summary

The three-dimensional solution structure of apo-neocarzinostatin has been resolved from nuclear magnetic resonance spectroscopy data. Up to 1034 constraints were used to generate an initial set of 45 structures using a distance geometry algorithm (DSPACE). From this set, ten structures were subjected to refinement by restrained energy minimization and molecular dynamics. The average atomic root mean square deviations between the final ten structures and the mean structure obtained by averaging their coordinates run from 0.085 nm for the best defined beta-sheet regions of the protein to 0.227 nm for the side chains of the most flexible loops. The solution structure of apo-neocarzinostatin is closely similar to that of the related proteins, macromomycin and actinoxanthin. It contains a seven-stranded antiparallel beta-barrel which forms, together with two external loops, a deep cavity that is the chromophore binding site. It is noteworthy that aromatic side chains extend into the binding cleft. They may be responsible for the stabilization of the holo-protein complex and for the chromophore specificity within the antitumoral family.

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Year of publication 1990

ADJADJ Élisabeth, MISPELTER Joël, QUINIOU Éric, DIMICOLI Jean-Luc, FAVAUDON Vincent, LHOSTE Jean-Marc (1990 Jun 20)

Proton NMR studies of apo-neocarzinostatin from Streptomyces carzinostaticus. Sequence-specific assignment and secondary structure.

European journal of biochemistry : 190 : 263-271 : DOI : 10.1111/j.1432-1033.1990.tb15571.x Learn more
Summary

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.

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