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1PJH

Structural studies on delta3-delta2-enoyl-CoA isomerase: the variable mode of assembly of the trimeric disks of the crotonase superfamily

Summary for 1PJH
Entry DOI10.2210/pdb1pjh/pdb
Related1HNO 1HNU
Descriptorenoyl-CoA isomerase; Eci1p, SULFATE ION, GLYCEROL, ... (4 entities in total)
Functional Keywordsbeta-beta-alpha spiral fold, inter-trimer contacts, isomerase
Biological sourceSaccharomyces cerevisiae (baker's yeast)
Cellular locationPeroxisome : Q05871
Total number of polymer chains3
Total formula weight96484.11
Authors
Mursula, A.M.,Hiltunen, J.K.,Wierenga, R.K. (deposition date: 2003-06-03, release date: 2004-01-20, Last modification date: 2023-08-16)
Primary citationMursula, A.M.,Hiltunen, J.K.,Wierenga, R.K.
Structural studies on delta(3)-delta(2)-enoyl-CoA isomerase: the variable mode of assembly of the trimeric disks of the crotonase superfamily.
Febs Lett., 557:81-87, 2004
Cited by
PubMed Abstract: 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.
PubMed: 14741345
DOI: 10.1016/S0014-5793(03)01450-9
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.1 Å)
Structure validation

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