   3.4.23.B24 | 2.4-A resolution structure of Bacillus subtilis SppA catalytic domain reveals eight SppA molecules in the asymmetric unit, forming a dome-shaped octameric complex. Residue Ser147 may serve as the nucleophile and Lys199 may serve as the general base. The SppA S1 substrate specificity pocket is deep, narrow and hydrophobic, but with a polar bottom. The S3 pocket, which is constructed from two neighboring proteins, is shallower, wider and more polar than the S1 pocket |
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| 3.4.23.B24 | crystal structure of a proteolytically stable fragment of mutant K199A, residues Leu51-Gly295, that has its C-terminal peptide bound in each of the eight active sites, creating a perfect circle of peptides. Substrate specificity pockets accommodate C-terminal residues Tyr331, Met329, and Tyr333, respectively. The C-terminus binds within the substrate-binding grooves in an antiparallel beta-sheet fashion |
733343 |
