ISSN:
0887-3585
Schlagwort(e):
β-glucosidases (family 3)
;
circular permutation
;
β/α-barrel
;
“mainly all-β” domain
;
double-domain topology
;
secondary-structure prediction
;
Chemistry
;
Biochemistry and Biotechnology
Quelle:
Wiley InterScience Backfile Collection 1832-2000
Thema:
Medizin
Notizen:
By predicting the general secondary structure for β-glucosidases (family 3), in conjunction with existing knowledge of the circular permutants present in B. fibrisolvens and R. albus, we were able to find the canonical elements of the secondary structure. The way these elements are linked suggests that there is a double-domain topology made up of a (β/α)8-barrel domain and a “mainly all-β” domain. A number of already known conserved motifs are located within (or near) the C-terminal part of the putative parallel β-strands of the (β/α)8-barrel, which is consistent with what is known about the location of catalytical sites for enzymes that have this domain topology. Within the circular permutants, two β/α units are located at the N-terminal part of the molecule, whereas the other six β/α units are located at the C-terminal end. In this way, the circular permutants can be seen to have a putative discontinuous double-domain topology. Proteins 31:214-223, 1998. © 1998 Wiley-Liss, Inc.
Zusätzliches Material:
3 Ill.
Materialart:
Digitale Medien
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