1SBC

THE REFINED CRYSTAL STRUCTURE OF SUBTILISIN CARLSBERG AT 2.5 ANGSTROMS RESOLUTION

1SBC の概要

• エントリーDOI: 10.2210/pdb1sbc/pdb
• 分子名称: SUBTILISIN CARLSBERG, CALCIUM ION (2 entities in total)
• 機能のキーワード: serine proteinase
• 由来する生物種: Bacillus subtilis
• 細胞内の位置: Secreted: P00780
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 27346.28

構造登録者

Neidhart, D.J.,Petsko, G.A. (登録日: 1988-05-13, 公開日: 1988-07-16, 最終更新日: 2024-02-14)

主引用文献

Neidhart, D.J.,Petsko, G.A.
The refined crystal structure of subtilisin Carlsberg at 2.5 A resolution.
Protein Eng., 2:271-276, 1988

PubMed Abstract: 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'.

PubMed: 3150541
DOI: 10.1093/protein/2.4.271

実験手法

X-RAY DIFFRACTION (2.5 Å)