1pjh
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Structural studies on delta3-delta2-enoyl-CoA isomerase: the variable mode of assembly of the trimeric disks of the crotonase superfamily
OverviewOverview
Subunits of the enzymes in the crotonase superfamily form tight trimeric, disks. In most members of this protein superfamily these disks assemble, further into hexamers. Here we report on the 2.1 A structure of a tight, hexameric crystal form of the yeast peroxisomal, delta(3)-delta(2)-enoyl-CoA isomerase (Eci1p). A comparison of this, structure to a previously solved crystal form of Eci1p and other, structures of this superfamily shows that there is much variability with, respect to the relative distance between the disks and their relative, orientations. In particular helices H2 and H9 are involved in the, inter-trimer contacts and there are considerable structural differences in, these helices in this superfamily. Helices H2 and H9 are near the, catalytic cavity and it is postulated that the observed structural, variability of these helices, stabilized by the different modes of, assembly, has allowed the evolution of the wide range of substrate and, catalytic specificity within this enzyme superfamily.
About this StructureAbout this Structure
1PJH is a Single protein structure of sequence from Saccharomyces cerevisiae with SO4 and GOL as ligands. Active as Dodecenoyl-CoA isomerase, with EC number 5.3.3.8 Full crystallographic information is available from OCA.
ReferenceReference
Structural studies on delta(3)-delta(2)-enoyl-CoA isomerase: the variable mode of assembly of the trimeric disks of the crotonase superfamily., Mursula AM, Hiltunen JK, Wierenga RK, FEBS Lett. 2004 Jan 16;557(1-3):81-7. PMID:14741345
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