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• W1490752921 abstract "The present 2.8 Å resolution structure determination of the microbial enzyme Streptomyces griseus protease A (SGPA) reveals a molecular architecture similar to that of the pancreatic serine proteases. The major structural dissimilarities between SGPA and the pancreatic enzymes are associated with the functional differences of these regions. Limited proteolytic cleavage of the zymogen precursors of the pancreatic proteases results in the formation of an ion-pair from the newly-formed amino-terminus to Asp194, and thereby in the active conformation of the enzymes. Inactive zymogen precursors for SGPA or other related bacterial serine proteases have not been reported. This is consistent with the present observations that the critical ion-pair involving the carboxylate group of Asp194 is formed permanently with the buried guanidinium group of Arg138. Although sequence homology between the bacterial serine proteases and the pancreatic enzymes is minimal (< 21%), the topological equivalence of the α-carbon atoms of SGPA and α-chymotrypsin is substantial (~60%, James et al., 1978). The residues in close proximity to the active site are most similar, not only in sequence but also in tertiary structure. In fact, we find almost identical conformations for the four residues of the active site (Ser214, Asp102, His57 and Ser195) to those found in the pancreatic enzymes. Although the carboxylate of Asp102 is buried, it is located in a highly polar environment as this group is the recipient of four hydrogen bonds. This fact indicates that the pKa of this group, were it directly measurable, would be considerably lower than expected for a freely available carboxylate moiety. The environment of Asp102 in SGPA is also similar to the environment of Asp32 of the acid protease penicillopepsin (Hsu et al., 1977) and the pKa of this latter carboxyl group is ~1.5. The Oγ of Ser195 is not in a position to form an ideal hydrogen bond to Nε2 of His57. The conformation of the seryl side-chain is the “down” position (χ1 ~ −80°) and we find no evidence for a conformation in which χ1 is different by ~180° from this value, as has been reported for native α-chymotrypsin (Birktoft & Blow, 1972). The overall degree of similarity of structure between SGPA and α-chymotrypsin leaves little doubt that these two enzyme families have a common ancestral origin." @default.
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• W1490752921 date "1978-09-01" @default.
• W1490752921 modified "2023-10-03" @default.
• W1490752921 title "Molecular structure of crystalline Streptomyces griseus protease A at 2.8 å resolution" @default.
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• W1490752921 doi "https://doi.org/10.1016/0022-2836(78)90159-6" @default.
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