Structural basis for Ca2+-independence and activation by homodimerization of tomato subtilase 3

Ottmann, C., Rose, R., Huttenlocher, F., Cedzich, A., Hauske, P., Kaiser, M., Huber, Robert and Schaller, A. 2009. Structural basis for Ca2+-independence and activation by homodimerization of tomato subtilase 3. Proceedings of the National Academy of Sciences 106 (40) , pp. 17223-17228. 10.1073/pnas.0907587106

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Abstract

Subtilases are serine proteases found in Archae, Bacteria, yeasts, and higher eukaryotes. Plants possess many more of these subtilisin-like endopeptidases than animals, e.g., 56 identified genes in Arabidopsis compared with only 9 in humans, indicating important roles for subtilases in plant biology. We report the first structure of a plant subtilase, SBT3 from tomato, in the active apo form and complexed with a chloromethylketone (cmk) inhibitor. The domain architecture comprises an N-terminal protease domain displaying a 132 aa protease-associated (PA) domain insertion and a C-terminal seven-stranded jelly-roll fibronectin (Fn) III-like domain. We present the first structural evidence for an explicit function of PA domains in proteases revealing a vital role in the homo-dimerization of SBT3 and in enzyme activation. Although Ca2+-binding sites are conserved and critical for stability in other subtilases, SBT3 was found to be Ca2+-free and its thermo stability is Ca2+-independent.

Item Type:	Article
Date Type:	Publication
Status:	Published
Schools:	Biosciences
Subjects:	Q Science > Q Science (General)
Uncontrolled Keywords:	calcium; proprotein convertase; protease-associated domain; subtilisin; thermostability
Publisher:	The National Academy of Sciences of the USA
ISSN:	0027-8424
Last Modified:	24 Jun 2017 08:51
URI:	https://orca.cardiff.ac.uk/id/eprint/22354

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