L-butaneboronic acid binding to Aeromonas proteolytica aminopeptidase:: A case of arrested development
L-butaneboronic acid binding to Aeromonas proteolytica aminopeptidase:: A case of arrested development
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DOI：
10.1021/bi9900572
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发表时间：
1999-07-13
期刊：
影响因子：
2.9
通讯作者：
Petsko, GA
中科院分区：
文献类型：
--
作者：
De Paola, CC;Bennett, B;Petsko, GA
Hydrolases containing two metal ions connected by a bridging ligand catalyze reactions important in carcinogensis, tissue repair, post-translational modification, control and regulation of biochemical pathways, and protein degradation. The aminopeptidase from Aeromonas proteolytica serves as a paradigm for the study of such bridged bimetallic proteases since its three-dimensional structure is known to very high resolution and its catalytic reaction is amenable to spectroscopic examination. Herein, we report, the X-ray crystal structure at 1.9 Angstrom resolution of AAP complexed with 1-butaneboronic acid (BuBA). This structure suggests that this complex represents a snapshot of the proteolytic reaction in an arrested form between the Michaelis complex and the transition state. Comparison of-the structure with spectroscopic and other data allows us to conclude that the apparently structurally symmetrical dizinc site is actually asymmetric: electrostatically.
