1spb
From Proteopedia
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SUBTILISIN BPN' PROSEGMENT (77 RESIDUES) COMPLEXED WITH A MUTANT SUBTILISIN BPN' (266 RESIDUES). CRYSTAL PH 4.6. CRYSTALLIZATION TEMPERATURE 20 C DIFFRACTION TEMPERATURE-160 C
Overview
BACKGROUND: The folding of the bacterial protease subtilisin BPN' (SBT) is, dependent on its 77-residue prosegment, which is then autocatalytically, removed to give the mature enzyme. Mature subtilisin represents a class of, proteins that lacks an efficient folding pathway. Refolding of mature SBT, is extremely slow unless catalyzed by the independently expressed, prosegment, leading to a bimolecular complex. RESULTS: We report the, crystal structure at 2.0 A resolution of the prosegment-SBT complex and, consider its implications for prosubtilisin BPN' maturation and folding, catalysis. The prosegment forms a compact domain that binds SBT through an, extensive interface involving the enzyme's two parallel surface helices, (residues 104-116 and 133-144), supplying negatively charged caps to the N, termini of these helices. The prosegment C terminus binds in the enzyme, active site in a product-like manner, with Tyr77 in the P1 binding pocket., CONCLUSIONS: The structure of the complex supports a unimolecular, mechanism for prosubtilisin cleavage, involving a 25 A rearrangement of, the SBT N terminus in a late folding step. A mechanism of folding, catalysis in which the two helices and their connecting beta strand form a, prosegment-stabilized folding nucleus is proposed. While this putative, nucleus is stabilized by prosegment binding, the N-terminal and C-terminal, subdomains of SBT could fold by propagation.
About this Structure
1SPB is a Single protein structure of sequence from Bacillus amyloliquefaciens with NA as ligand. Active as Subtilisin, with EC number 3.4.21.62 Full crystallographic information is available from OCA.
Reference
The prosegment-subtilisin BPN' complex: crystal structure of a specific 'foldase'., Gallagher T, Gilliland G, Wang L, Bryan P, Structure. 1995 Sep 15;3(9):907-14. PMID:8535784
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