TY - JOUR
T1 - Structural analysis shows five glycohydrolase families diverged from a common ancestor
AU - Robertus, Jond D.
AU - Monzingo, Arthur F.
AU - Marcotte, Edward M.
AU - Hart, P. John
N1 - Copyright:
Copyright 2020 Elsevier B.V., All rights reserved.
PY - 1998/9
Y1 - 1998/9
N2 - We have solved the X-ray structure of barley chitinase and bacterial chitosanase. Structural constraints predicted these would work by an inverting mechanism, which has been confirmed biochemically. The two enzymes were compared with lysozymes from goose (GEWL), phage (T4L), and hen (HEWL). Although the proteins share no significant amino acid similarities, they are shown to have a structurally invariant core containing two helices and a three-stranded sheet that form the substrate binding and catalytic cleft. These enzymes represent a superfamily of hydrolases arising from the divergent evolution of an ancient protein. The glycohydrolase superfamily can be structurally divided into a bacterial family (chitosanase and T4L), and a eucaryotic family represented by chitinase, GEWL, and HEWL. Both families contain the ancestral core but differ at the amino and carboxy termini. The eucaryotes have a small N terminal domain, while the procaryotes have none. The C terminal domain of the eucaryotic family contains a single α-helix, while the prokaryotic domain has three antiparallel helices.
AB - We have solved the X-ray structure of barley chitinase and bacterial chitosanase. Structural constraints predicted these would work by an inverting mechanism, which has been confirmed biochemically. The two enzymes were compared with lysozymes from goose (GEWL), phage (T4L), and hen (HEWL). Although the proteins share no significant amino acid similarities, they are shown to have a structurally invariant core containing two helices and a three-stranded sheet that form the substrate binding and catalytic cleft. These enzymes represent a superfamily of hydrolases arising from the divergent evolution of an ancient protein. The glycohydrolase superfamily can be structurally divided into a bacterial family (chitosanase and T4L), and a eucaryotic family represented by chitinase, GEWL, and HEWL. Both families contain the ancestral core but differ at the amino and carboxy termini. The eucaryotes have a small N terminal domain, while the procaryotes have none. The C terminal domain of the eucaryotic family contains a single α-helix, while the prokaryotic domain has three antiparallel helices.
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U2 - 10.1002/(sici)1097-010x(199809/10)282:1/2<127::aid-jez14>3.0.co;2-r
DO - 10.1002/(sici)1097-010x(199809/10)282:1/2<127::aid-jez14>3.0.co;2-r
M3 - Article
C2 - 9723170
AN - SCOPUS:3543043078
VL - 282
SP - 127
EP - 132
JO - Journal of Experimental Zoology Part B: Molecular and Developmental Evolution
JF - Journal of Experimental Zoology Part B: Molecular and Developmental Evolution
SN - 0022-104X
IS - 1-2
ER -