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Preliminary X‐ray diffraction studies and biochemical characterization of the antitumor protein mitomalcin indicate close similarity to neocarzinostatin
Author(s) -
Sieker L. C.,
Gnanarajah G. G.
Publication year - 1988
Publication title -
proteins: structure, function, and bioinformatics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.699
H-Index - 191
eISSN - 1097-0134
pISSN - 0887-3585
DOI - 10.1002/prot.340030406
Subject(s) - neocarzinostatin , molecule , streptomyces , biochemistry , chemistry , x ray crystallography , sequence (biology) , stereochemistry , biology , crystallography , bacteria , diffraction , dna , organic chemistry , physics , optics , genetics
The antitumor antibiotic protein mitomalcin, from the microorganism Streptomyces malayensis , has been purified to apparent homogenity and crystallized. The crystals belong to space group P2 1 2 1 2 1 and have the following cell parameters : a=27.2 Å, b=34.1 Å, c=101.7 Å, and alpha;=β=γ=90°. These crystal properties are extremely similar to crystals of the antitumor protein neocarzinostatin (11.7 kilodaltons [kDa]) from Streptomyces carzinostaticus in spite of differing pH conditions for crystallizing the two proteins and an apparent difference in molecular weight is similar to that of neocarzinostatin. An amino acid composition analysis of mitomalcin indicates that some differences may exist between the two molecules, but a preliminary amino acid sequence analysis of the first 37 residues found no difference in the N‐terminal region of the molecule.