Article (Scientific journals)
The Noncatalytic Triad of Alpha-Amylases: A Novel Structural Motif Involved in Conformational Stability
Marx, J. C.; Poncin, J.; Simorre, J. P. et al.
2008In Proteins, 70 (2), p. 320-328
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Abstract :
[en] Chloride-activated alpha-amylases contain a noncatalytic triad, independent of the glycosidic active site, perfectly mimicking the catalytic triad of serine-proteases and of other active serine hydrolytic enzymes. Mutagenesis of Glu, His, and Ser residues in various alpha-amylases shows that this pattern is a structural determinant of the enzyme conformation that cannot be altered without losing the intrinsic stability of the protein. (1)H-(15)N NMR spectra of a bacterial alpha-amylase reveal proton signals that are identical with the NMR signature of catalytic triads and especially a deshielded proton involving a protonated histidine and displaying properties similar to that of a low barrier hydrogen bond. It is proposed that the H-bond between His and Glu of the noncatalytic triad is an unusually strong interaction, responsible for the observed NMR signal and for the weak stability of the triad mutants. Furthermore, a stringent template-based search of the Protein Data Bank demonstrated that this motif is not restricted to alpha-amylases, but is also found in 80 structures from 33 different proteins, amongst which SH2 domain-containing proteins are the best representatives.
Disciplines :
Biochemistry, biophysics & molecular biology
Author, co-author :
Marx, J. C.
Poncin, J.
Simorre, J. P.
Ramteke, P. W.
Feller, Georges ;  Université de Liège - ULiège > Département des sciences de la vie > Labo de biochimie
Language :
English
Title :
The Noncatalytic Triad of Alpha-Amylases: A Novel Structural Motif Involved in Conformational Stability
Publication date :
01 February 2008
Journal title :
Proteins
ISSN :
0887-3585
eISSN :
1097-0134
Publisher :
Wiley-Liss Inc, United States - New York
Volume :
70
Issue :
2
Pages :
320-328
Peer reviewed :
Peer Reviewed verified by ORBi
Available on ORBi :
since 26 January 2010

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