SUBTILISIN BPN' AT 1.6-ANGSTROM RESOLUTION - ANALYSIS FOR DISCRETE DISORDER AND COMPARISON OF CRYSTAL FORMS

Citation
T. Gallagher et al., SUBTILISIN BPN' AT 1.6-ANGSTROM RESOLUTION - ANALYSIS FOR DISCRETE DISORDER AND COMPARISON OF CRYSTAL FORMS, Acta crystallographica. Section D, Biological crystallography, 52, 1996, pp. 1125-1135
Citations number
33
Language
INGLESE
art.tipo
Article
Categorie Soggetti
Crystallography,"Biochemical Research Methods",Biology
ISSN journal
0907-4449
Volume
52
Year of publication
1996
Part
6
Pages
1125 - 1135
Database
ISI
SICI code
0907-4449(1996)52:<1125:SBA1R->2.0.ZU;2-F
Abstract
The three-dimensional structure of the serine protease subtilisin BPN' (SET) has been refined at 1.6 Angstrom resolution in space group C2 t o a final R value of 0.17. 17 regions of discrete disorder have been i dentified and analyzed. Two of these are dual-conformation peptide uni ts; the remainder involve alternate rotamers of side chains either alo ne or in small clusters. The structure is compared with previously rep orted high-resolution models of SET in two other space groups, P2(1)2( 1)2(1) and P2(1). Apart from the surface, there are no significant var iations in structure among the three crystal forms. Structural variati ons observed at the protein surface occur predominantly in regions of protein-protein contact. The crystal packing arrangements in the three space groups are compared.