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Biochim Biophys Acta. 1999 Nov 23;1441(2-3):237-54.

Bacterial phosphatidylinositol-specific phospholipase C: structure, function, and interaction with lipids.

Author information

1
Institute of Molecular Biology and Department of Chemistry, University of Oregon, Eugene, OR 97403, USA. hayes@molbio.uoregon.edu

Abstract

The bacterial phosphatidylinositol-specific phospholipase C (PI-PLC) is a small, water-soluble enzyme that cleaves the natural membrane lipids PI, lyso-PI, and glycosyl-PI. The crystal structure, NMR and enzymatic mechanism of bacterial PI-PLCs are reviewed. These enzymes consist of a single domain folded as a (betaalpha)(8)-barrel (TIM barrel), are calcium-independent, and interact weakly with membranes. Sequence similarity among PI-PLCs from different bacterial species is extensive, and includes the residues involved in catalysis. Bacterial PI-PLCs are structurally similar to the catalytic domain of mammalian PI-PLCs. Comparative studies of both prokaryotic and eukaryotic isozymes have proved useful for the identification of distinct regions of the proteins that are structurally and functionally important.

PMID:
10570252
DOI:
10.1016/s1388-1981(99)00153-5
[Indexed for MEDLINE]

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