2ZW7

Crystal structure of bleomycin N-acetyltransferase complexed with bleomycin A2 and coenzyme A

Summary for 2ZW7

• Entry DOI: 10.2210/pdb2zw7/pdb
• Related: 2ZW4 2ZW5 2ZW6
• Descriptor: Bleomycin acetyltransferase, COENZYME A, BLEOMYCIN A2, ... (4 entities in total)
• Functional Keywords: dimer, two domains, transferase
• Biological source: Streptomyces verticillus
• Total number of polymer chains: 2
• Total formula weight: 68518.90

Authors

Oda, K.,Matoba, Y.,Sugiyama, M. (deposition date: 2008-12-01, release date: 2009-11-03, Last modification date: 2023-11-15)

Primary citation

Oda, K.,Matoba, Y.,Noda, M.,Kumagai, T.,Sugiyama, M.
Catalytic mechanism of bleomycin N-acetyltransferase proposed on the basis of its crystal structure.
J.Biol.Chem., 285:1446-1456, 2010

PubMed Abstract: Bleomycin (Bm) N-acetyltransferase, BAT, is a self-resistance determinant in Bm-producing Streptomyces verticillus ATCC15003. In our present study, we crystallized BAT under both a terrestrial and a microgravity environment in the International Space Station. In addition to substrate-free BAT, the crystal structures of BAT in a binary complex with CoA and in a ternary complex with Bm and CoA were determined. BAT forms a dimer structure via interaction of its C-terminal domains in the monomers. However, each N-terminal domain in the dimer is positioned without mutual interaction. The tunnel observed in the N-terminal domain of BAT has two entrances: one that adopts a wide funnel-like structure necessary to accommodate the metal-binding domain of Bm, and another narrow entrance that accommodates acetyl-CoA (AcCoA). A groove formed on the dimer interface of two BAT C-terminal domains accommodates the DNA-binding domain of Bm. In a ternary complex of BAT, BmA(2), and CoA, a thiol group of CoA is positioned near the primary amine of Bm at the midpoint of the tunnel. This proximity ensures efficient transfer of an acetyl group from AcCoA to the primary amine of Bm. Based on the BAT crystal structure and the enzymatic kinetic study, we propose that the catalytic mode of BAT takes an ordered-like mechanism.

PubMed: 19889644
DOI: 10.1074/jbc.M109.022277

Experimental method

X-RAY DIFFRACTION (2.8 Å)