1ugt
From Proteopedia
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Structural Studies of Cu(I)-Bleomycin
Overview
Previous NMR studies on Cu(I)-bleomycin have suggested that this adduct, has a geometry distinct from Fe(II)BLM. The coordination chemistry of this, bleomycin derivative has been investigated through the extension of the, NMR data reported previously, and the use of molecular dynamics, calculations. The data collected from the NMR experiments support the, coordination to the metal center of the primary and secondary amines in, beta-aminoalanine and the pyrimidine ring. The detection in the NMR, spectra of the signal derived from the amide hydrogen in, beta-hydroxyhistidine indicates that this amide is protonated in, Cu(I)-bleomycin, precluding participation of the pyrimidinyl carboxamide, nitrogen in the coordination of Cu(I), as previously reported., Three-dimensional solution structures compatible with the NMR data have, been assayed for Cu(I)-bleomycin for the first time by way of molecular, dynamics calculations, and two models showing four and five coordination, have been found to be those that better fit the experimental data. In both, models the primary amine in beta-aminoalanine is coordinated such that it, is located on the same side, with respect to the coordination cage, as the, peptide linker fragment. This result seems important for the favored, models to be compatible with either their possible oxidation to become one, of the reported structures for Cu(II)BLM, or their transformation into, Fe(II) adducts able to cause DNA damage.
About this Structure
1UGT is a Protein complex structure of sequences from [1] with CO and BLM as ligands. Full crystallographic information is available from OCA.
Reference
Structural study of copper(I)-bleomycin., Lehmann TE, J Biol Inorg Chem. 2004 Apr;9(3):323-34. Epub 2004 Mar 10. PMID:15015041
Page seeded by OCA on Sun Nov 25 03:58:35 2007
Categories: Protein complex | Lehmann, T.E. | BLM | CO | Metal complex
