Desmarais William, Bienvenue David L, Bzymek Krzysztof P, Petsko Gregory A, Ringe Dagmar, Holz Richard C
Program in Biophysics and Structural Biology, Brandeis University, 415 South Street, Waltham, MA 02254-9110, USA.
J Biol Inorg Chem. 2006 Jun;11(4):398-408. doi: 10.1007/s00775-006-0093-x. Epub 2006 Apr 5.
The aminopeptidase from Aeromonas proteolytica (AAP) contains two zinc ions in the active site and catalyzes the degradation of peptides. Herein we report the crystal structures of AAP at 0.95-A resolution at neutral pH and at 1.24-A resolution at low pH. The combination of these structures allowed the precise modeling of atomic positions, the identification of the metal bridging oxygen species, and insight into the physical properties of the metal ions. On the basis of these structures, a new putative catalytic mechanism is proposed for AAP that is likely relevant to all binuclear metalloproteases.
解蛋白气单胞菌的氨肽酶（AAP）在活性位点含有两个锌离子，并催化肽的降解。在此，我们报告了AAP在中性pH下0.95埃分辨率和低pH下1.24埃分辨率的晶体结构。这些结构的结合使得能够精确模拟原子位置、识别金属桥连氧物种，并深入了解金属离子的物理性质。基于这些结构，我们提出了一种新的AAP推定催化机制，该机制可能与所有双核金属蛋白酶相关。
