Structural highlights
Function
CHIB_SERMA
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
The crystal structure of the inactive D140N mutant of Serratia marcescens was refined to 1.45 A resolution. The structure of the mutant was essentially identical to that of the wild type, with the exception of a rotation of Asp142 in the catalytic centre. In the mutant, this residue interacts with the catalytic acid (Glu144) and not with residue 140 as in the wild type. Thus, the 500-fold decrease in activity in the D140N mutant seems to be largely mediated by an effect on Asp142, confirming the crucial role of the latter residue in catalysis.
Structure of the D140N mutant of chitinase B from Serratia marcescens at 1.45 A resolution.,Kolstad G, Synstad B, Eijsink VG, van Aalten DM Acta Crystallogr D Biol Crystallogr. 2002 Feb;58(Pt 2):377-9. Epub 2002, Jan 24. PMID:11807282[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Kolstad G, Synstad B, Eijsink VG, van Aalten DM. Structure of the D140N mutant of chitinase B from Serratia marcescens at 1.45 A resolution. Acta Crystallogr D Biol Crystallogr. 2002 Feb;58(Pt 2):377-9. Epub 2002, Jan 24. PMID:11807282
