1JIE

Crystal structure of bleomycin-binding protein from bleomycin-producing Streptomyces verticillus complexed with metal-free bleomycin

Summary for 1JIE

• Entry DOI: 10.2210/pdb1jie/pdb
• Related: 1ECS 1EWJ 1JIF 1QTO
• Descriptor: bleomycin-binding protein, BLEOMYCIN A2 (3 entities in total)
• Functional Keywords: protein-ligand complex, protein binding
• Biological source: Streptomyces verticillus
• Total number of polymer chains: 2
• Total formula weight: 29320.33

Authors

Sugiyama, M.,Kumagai, T.,Hayashida, M.,Maruyama, M.,Matoba, Y. (deposition date: 2001-07-02, release date: 2002-02-06, Last modification date: 2023-10-25)

Primary citation

Sugiyama, M.,Kumagai, T.,Hayashida, M.,Maruyama, M.,Matoba, Y.
The 1.6-A crystal structure of the copper(II)-bound bleomycin complexed with the bleomycin-binding protein from bleomycin-producing Streptomyces verticillus.
J.Biol.Chem., 277:2311-2320, 2002

PubMed Abstract: Bleomycin (Bm) in the culture broth of Streptomyces verticillus is complexed with Cu(2+) (Cu(II)). In the present study, we determined the x-ray crystal structures of the Cu(II)-bound and the metal-free types of Bm at a high resolution of 1.6 and 1.8 A, respectively, which are complexed with a Bm resistance determinant from Bm-producing S. verticillus, designated BLMA. In the current model of Cu(II).Bm complexed with BLMA, two Cu(II).Bm molecules bind to the BLMA dimer. The electron density map shows that the copper ion is clearly defined in the metal-binding domain of the Bm molecule. The metal ion is penta-coordinated by a tetragonal monopyramidal cage of nitrogens and binds to the primary amine of the beta-aminoalanine moiety of Bm. The binding experiment between Bm and BLMA showed that each of the two Bm-binding pockets has a different dissociation constant (K(d)(1) and K(d)(2)). The K(d)(1) value of 630 nm for the first Bm binding is larger than the K(d)(2) value of 120 nm, indicating that the first Bm binding gives rise to a cooperative binding of the second Bm to the other pocket.

PubMed: 11706014
DOI: 10.1074/jbc.M103278200

Experimental method

X-RAY DIFFRACTION (1.8 Å)