Open AccessThree‐dimensional solution structure of apo‐neocarzinostatin from Streptomyces carzinostaticus determined by NMR spectroscopy
Author(s) -
ADJADJ Élisabeth,
QUINIOU Éric,
MISPELTER Joël,
FAVAUDON Vincent,
LHOSTE JeanMarc
Publication year - 1992
Publication title -
european journal of biochemistry
Language(s) - English
Resource type - Journals
eISSN - 1432-1033
pISSN - 0014-2956
DOI - 10.1111/j.1432-1033.1992.tb16576.x
Subject(s) - antiparallel (mathematics) , chromophore , planarity testing , neocarzinostatin , crystallography , nuclear magnetic resonance spectroscopy , chemistry , spectroscopy , energy minimization , side chain , molecular dynamics , two dimensional nuclear magnetic resonance spectroscopy , stereochemistry , physics , computational chemistry , photochemistry , polymer , dna , biochemistry , quantum mechanics , magnetic field , organic chemistry
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 β‐sheet regions of the protein to 0.227 nm for the side chains of the most flexible loops. The solution structure of aponeocarzinostatin is closely similar to that of the related proteins, macromomycin and actinoxanthin. It contains a seven‐stranded antiparallel β‐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.