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The 1.35 Å structure of cadmium-substituted TM-3, a snake-venom metalloproteinase from Taiwan habu: elucidation of a TNFα-converting enzyme-like active-site structure with a distorted octahedral geometry of cadmium by Kai-Fa Huang; Shyh-Horng Chiou; Tzu-Ping Ko; Jeu-Ming Yuann; Andrew H.-J. Wang is a Biochemistry, Genetics and Molecular Biology article available to read on EtoBox.

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The crystal structure of TM-3, a small snake-venom metalloproteinase (SVMP) isolated from Taiwan habu (Trimeresurus mucrosquamatus), was determined at 1.35 A resolution with resultant R and R(free) values of 0.181 and 0.204, respectively. The overall structure of TM-3 is an oblate ellipsoid that contains three disulfide crosslinks, Cys118-Cys197, Cys159-Cys181 and Cys161-Cys164. It exhibits the typical structural features of SVMPs and is closely related to the structure of the catalytic proteinase domain of TNFalpha-converting enzyme (TACE). In the present structure, the essential catalytic zinc ion was found to be replaced by a cadmium ion during crystallization, as revealed by atomic absorption analysis and X-ray data. This cadmium ion is bound to six ligands, including three conserved histidines and three water molecules, displaying the coordination geometry of a distorted octahedron. One of the water molecules is proposed to play the role of stabilizing the tetrahedral intermediate during the catalysis of SVMPs. The putative S'(1) specificity pocket of TM-3 is relatively shallow, in contrast to the deep pockets of adamalysin II, atrolysin C and H(2)-proteinase, but is similar t

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Author

Kai-Fa Huang; Shyh-Horng Chiou; Tzu-Ping Ko; Jeu-Ming Yuann; Andrew H.-J. Wang

Publisher

International Union of Crystallography; Blackwell Publishing Inc.; International Union of Crystallography (IUCr) (ISSN 0907-4449)

Published

2002

Language

EN

Field

Biochemistry, Genetics and Molecular Biology (Life Sciences)