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The catalytic domain of the P-type ATPase has the haloacid dehalogenase fold

Authors :
Aravind, L.
Galperin, Michael Y.
Koonin, Eugene V.
Source :
Trends in Biochemical Sciences. April, 1998, Vol. 23 Issue 4, p127, 3 p.
Publication Year :
1998

Abstract

The P-type ATPases belong to a superfamily of hydrolases whose structure is typified by the L-2-haloacid dehalogenase (HAD) 7,8 from Pseudomonas sp. The catalytic mechanism of P-type ATPases and HAD 7,8 are similar, providing clues to the evolution of these enzymes. The catalytic domain of P-type ATPases has been found to have the structural fold of haloacid dehalogenases. Thus, P-type ATPases might have evolved by fusion of a transmembrane protein with a HAD superfamily phosphatase domain.

Details

ISSN :
09680004
Volume :
23
Issue :
4
Database :
Gale General OneFile
Journal :
Trends in Biochemical Sciences
Publication Type :
Academic Journal
Accession number :
edsgcl.20742201