CRYSTALLOGRAPHIC STRUCTURE DETERMINATION OF PRO REGION OF A LYTIC PROTEASE

α-裂解蛋白酶是一种198个氨基酸的细菌丝氨酸蛋白酶 由产酶溶杆菌分泌。 在分泌之前， 作为40 kD前体存在，由信号序列、PRO 区域，以及最终成为活跃区域的成熟区域。 蛋白酶 一些研究表明，PRO区域是 在体外和体内都需要适当的折叠， 蛋白酶 在体内，表达的没有PRO区的蛋白酶是 不是秘密的。 在体外，变性蛋白酶不会再折叠， 增加PRO区域。 PRO区域也是亚纳摩尔的 天然酶的抑制剂。 很明显， PRO区和成熟蛋白酶之间的差异是广泛的， 揭示了蛋白质如何折叠以及为什么a-裂解不能折叠 本身 我们将研究PRO区域的晶体。

a-lytic protease is a 198 amino acid bacterial serine protease that is secreted from Lysobacter enzymogenes. Before secretion it exists as a 40 kD precursor, consisting of a signal sequence, a PRO region, and the mature domain that eventually becomes the active protease. A number of studies have shown that the PRO region is required both in vitro and in vivo for proper folding of a-lytic protease. In vivo the protease expressed without the PRO region is not secreted. In vitro the denatured protease will not refold without the addition of PRO region. The PRO region is also a sub-nanomolar inhibitor of the native enzyme. It is clear that the interactions between the PRO region and the mature protease are extensive and may shed some light on how proteins fold and why a-lytic cannot fold by itself. We will be studying crystals of the PRO region.