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Page 1

Biology of Inositols
and Phosphoinositides
Subcellular Biochemistry
Volume 39

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J. ROBIN HARRIS, University of Mainz, Mainz, Germany


B.B. BISWAS, University of Calcutta, Calcutta, India

P. QUINN, King's College London, London, U.K

Recent Volumes in this Series

Volume 31 Intermediate Filaments
Edited by Harald Herrmann and J. Robin Harris

Volume 32 alpha-Gal and Anti-Gal: alpha-1,3-Galactosyltransferase, alpha-Gal
Epitopes and the Natural Anti-Gal Antibody
Edited by Uri Galili and Jos-Luis Avila

Volume 33 Bacterial Invasion into Eukaryotic Cells
Tobias A. Oelschlaeger and Jorg Hacker

Volume 34 Fusion of Biological Membranes and Related Problems
Edited by Herwig Hilderson and Stefan Fuller

Volume 35 Enzyme-Catalyzed Electron and Radical Transfer
Andreas Holzenburg and Nigel S. Scrutton

Volume 36 Phospholipid Metabolism in Apoptosis
Edited by Peter J. Quinn and Valerian E. Kagan

Volume 37 Membrane Dynamics and Domains
Edited by P.J. Quinn

Volume 38 Alzheimer’s Disease: Cellular and Molecular Aspects of Amyloid beta
Edited by R. Harris and F. Fahrenholz

Page 173

of the molecule, mostly involving residues from the central domain. While the

sheet interaction buries 6,000 Å2 of surface area in yMIPS, the more exten-
sive interface in yMIPS stretching from bottom to top of the molecule buries
11,700 Å2 of surface area (Stein and Geiger, 2002). Since both of these inter-
faces are relatively hydrophobic, stable dissociation of the tetramer is highly
unlikely. Though there are several reports indicating some eukaryotic MIPS
enzymes to be trimeric in solution (Gumber et al., 1984; Maeda and Eisen-
berg, 1980; Ogunyemi et al., 1978; Raychaudhuri et al., 1997), the high

164 J.H. Geiger and X. Jin

Figure 3. Sequence alignment of MIPS from several sources. Elements of secondary structure as
defined in yMIPS are shown above the alignment and numbered. Cylinders are helices and wide

Page 174

sequence identity between MIPS from higher eukaryotes (approximately 50%
identity between yMIPS and all known eukaryotic sequences) and the two
extensive interfaces seen in yMIPS lead to the conclusion that all eukaryotic
MIPS are likely to be tetrameric. Both aMIPS and mMIPS tetramers are rela-
tively similar to the yMIPS tetramer, characterized by the packing of
and strand-to-strand interaction of
strands between protomers. It would
appear that the oligomerization state of the enzyme has been conserved
throughout evolution. The most notable differences between the structures lay
in the central domain region. Both aMIPS and mMIPS lack the n-terminal
region and the Rossman fold insertion that largely make up this domain. The
result is that both aMIPS and mMIPS have significantly smaller interfaces
between protomers in this interface (Norman et al., 2002; Stein and Geiger,
2002; Stieglitz et al., 2004).

The structure and mechanism of myo-inositol-1-phosphate synthase 165

Figure 3. (continued)

Page 346

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