1sbc
From Proteopedia
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THE REFINED CRYSTAL STRUCTURE OF SUBTILISIN CARLSBERG AT 2.5 ANGSTROMS RESOLUTION
Overview
We report here the X-ray crystal structure of native subtilisin Carlsberg, solved at 2.5 A resolution by molecular replacement and refined by, restrained least squares to a crystallographic residual (Formula see, text): of 0.206. we compare this structure to the crystal structure of, subtilisin BPN'. We find that, despite 82 amino acid substitutions and one, deletion in subtilisin Carlsberg relative to subtilisin BPN', the, structures of these enzymes are remarkably similar. We calculate an r.m.s., difference between equivalent alpha-carbon positions in subtilisin, Carlsberg and subtilisin BPN' of only 0.55 A. This confirms previous, reports of extensive structural homology between these two subtilisins, based on X-ray crystal structures of the complex of eglin-c with, subtilisin Carlsberg [McPhalen, C.A., Schnebli, H.P. and James, M.N.G., (1985) FEBS Lett., 188, 55; Bode, W., Papamokos, E. and Musil, D. (1987), Eur. J. Biochem., 166, 673-692]. In addition, we find that the native, active sites of subtilisins Carlsberg and BPN' are virtually identical., While conservative substitutions at residues 217 and 156 may have subtle, effects on the environments of substrate-binding sites S1' and S1, respectively, we find no obvious structural correlate for reports that, subtilisins Carlsberg and BPN' differ in their recognition of model, substrates. In particular, we find no evidence that the hydrophobic, binding pocket S1 in subtilisin Carlsberg is 'deeper', 'narrower' or 'less, polar' than the corresponding binding site in subtilisin BPN'.
About this Structure
1SBC is a Single protein structure of sequence from Bacillus subtilis with CA as ligand. Active as Subtilisin, with EC number 3.4.21.62 Full crystallographic information is available from OCA.
Reference
The refined crystal structure of subtilisin Carlsberg at 2.5 A resolution., Neidhart DJ, Petsko GA, Protein Eng. 1988 Oct;2(4):271-6. PMID:3150541
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