Baumann U
Abteilung für Strukturforschung, Max-Planck-Institut für Biochemie, Martinsried, Germany.
J Mol Biol. 1994 Sep 23;242(3):244-51. doi: 10.1006/jmbi.1994.1576.
The crystal structure of the 50 kDa metalloprotease from the Gram-negative bacterium Serratia marcescens has been solved and refined to a crystallographic R-factor of 0.192 at 1.80 A resolution. The structure is very similar to that of alkaline protease from Pseudomonas aeruginosa, in particular the calcium binding "parallel beta roll" motif is completely conserved. The N-terminal proteolytic domain shows the typical "metzincin" fold. The active sites of the two enzymes are slightly different, Tyr216 is a Zn ligand in the Serratia metallo protease. The loops 70-77 and 122-132, which encompass the active site cleft, differ due to insertions and deletions so that the Serratia metallo protease seems to have a more open site than the alkaline protease.
来自革兰氏阴性菌粘质沙雷氏菌的50 kDa金属蛋白酶的晶体结构已被解析，并在1.80 Å分辨率下精修至晶体学R因子为0.192。该结构与铜绿假单胞菌碱性蛋白酶的结构非常相似，特别是钙结合“平行β折叠”基序完全保守。N端蛋白水解结构域呈现典型的“金属锌酶”折叠。这两种酶的活性位点略有不同，在粘质沙雷氏菌金属蛋白酶中，Tyr216是锌配体。包含活性位点裂隙的70 - 77环和122 - 132环因插入和缺失而不同，因此粘质沙雷氏菌金属蛋白酶的位点似乎比碱性蛋白酶的位点更开放。
