1ao4

From Proteopedia

proteopedia linkproteopedia link

spinqualitylabelsall models 1ao4 Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

COBALT(III)-PEPLOMYCIN COMPLEX DETERMINED BY NMR STUDIES

Overview

Pepleomycin (PEP) is a metalloglycopeptide that has stronger anticancer, activity and less pulmonary toxicity than bleomycin (BLM). PEP, like BLM, exerts its action by binding to and degrading DNA in the presence of, oxygen and certain metals. Obtaining detailed structural information of, PEP and PEP-DNA complexes is crucial to understanding its anticancer, activity. The structures of two green forms of cobalt-PEP species, HO2-Co(III)-PEP (denoted CoPEP) and deglycosylated HO2-Co(III)-PEP, (denoted CodPEP) have been obtained by NOE restrained refinements. Earlier, studies of the related HO2-Co(III)-BLM A2 proposed that two chiral, conformers (form A or B) could exist with either the beta-aminoalanine, primary amine (A,NH2) or the mannose carbamoyl nitrogen (M,NH2) as the, axial ligand. Analysis of our NOESY data shows convincingly that form A is, the most probable conformer with the mannose carbamoyl M,NH2 and the, beta-aminoalanine primary amine A,NH2 as the axial ligands in CoPEP and, CodPEP, respectively. The NOE cross-peaks resulting from the interactions, between the N-terminus (i.e., the metal-binding domain) and the C-terminus, of CoPEP and CodPEP have similar patterns, suggesting that they both adopt, compact structures with the bithiazole group folded back over the, N-terminus.

About this Structure

1AO4 is a Protein complex structure of sequences from [1] with 3CO, PMY and PEO as ligands. Full crystallographic information is available from OCA.

Reference

Structures of cobalt(III)-pepleomycin and cobalt(III)-deglycopepleomycin (green forms) determined by NMR studies., Caceres-Cortes J, Sugiyama H, Ikudome K, Saito I, Wang AH, Eur J Biochem. 1997 Mar 15;244(3):818-28. PMID:9108252

Page seeded by OCA on Sat Nov 24 23:07:57 2007