Kawasaki Akio, Nakano Hiroaki, Tsujimoto Yoshiyuki, Matsui Hiroshi, Shimizu Tetsuya, Nakatsu Toru, Kato Hiroaki, Watanabe Kunihiko
Department of Applied Biochemistry, Kyoto Prefectural University, Shimogamo, Sakyo, Kyoto 606-8522, Japan.
Acta Crystallogr Sect F Struct Biol Cryst Commun. 2007 Feb 1;63(Pt 2):142-4. doi: 10.1107/S174430910700334X. Epub 2007 Jan 27.
Pz peptidase A is an intracellular M3 metallopeptidase found in the thermophile Geobacillus collagenovorans MO-1 that recognizes collagen-specific tripeptide units (Gly-Pro-Xaa). Pz peptidase A shares common reactions with mammalian thimet oligopeptidase (TOP) and neurolysin, but has extremely low primary sequence identity to these enzymes. In this work, Pz peptidase A was cocrystallized with a phosphine peptide inhibitor (PPI) that selectively inhibits TOP and neurolysin. The crystals belong to space group P2(1), with unit-cell parameters a = 56.38, b = 194.15, c = 59.93 A, beta = 106.22 degrees . This is the first crystallographic study of an M3 family peptidase-PPI complex.
Pz肽酶A是一种细胞内M3金属肽酶，存在于嗜热菌嗜胶原地芽孢杆菌MO-1中，可识别胶原蛋白特异性三肽单元（甘氨酸-脯氨酸-Xaa）。Pz肽酶A与哺乳动物的硫醇寡肽酶（TOP）和神经溶素具有共同的反应，但与这些酶的一级序列同源性极低。在这项研究中，Pz肽酶A与一种选择性抑制TOP和神经溶素的膦肽抑制剂（PPI）共结晶。晶体属于空间群P2(1)，晶胞参数为a = 56.38，b = 194.15，c = 59.93 Å，β = 106.22°。这是对M3家族肽酶-PPI复合物的首次晶体学研究。
