1DCI
DIENOYL-COA ISOMERASE
Summary for 1DCI
Entry DOI | 10.2210/pdb1dci/pdb |
Descriptor | DIENOYL-COA ISOMERASE, SULFATE ION, MAGNESIUM ION, ... (5 entities in total) |
Functional Keywords | lyase, dienoyl-coa isomerase |
Biological source | Rattus norvegicus (Norway rat) |
Cellular location | Mitochondrion: Q62651 |
Total number of polymer chains | 3 |
Total formula weight | 92548.37 |
Authors | Modis, Y.,Filppula, S.A.,Novikov, D.,Norledge, B.,Hiltunen, J.K.,Wierenga, R.K. (deposition date: 1998-02-13, release date: 1999-03-30, Last modification date: 2024-02-07) |
Primary citation | Modis, Y.,Filppula, S.A.,Novikov, D.K.,Norledge, B.,Hiltunen, J.K.,Wierenga, R.K. The crystal structure of dienoyl-CoA isomerase at 1.5 A resolution reveals the importance of aspartate and glutamate sidechains for catalysis. Structure, 6:957-970, 1998 Cited by PubMed Abstract: The degradation of unsaturated fatty acids is vital to all living organisms. Certain unsaturated fatty acids must be catabolized via a pathway auxiliary to the main beta-oxidation pathway. Dienoyl-coenzyme A (dienoyl-CoA) isomerase catalyzes one step of this auxiliary pathway, the isomerization of 3-trans,5-cis-dienoyl-CoA to 2-trans,4-trans-dienoyl-CoA, and is imported into both mitochondria and peroxisomes. Dienoyl-CoA isomerase belongs to a family of CoA-binding proteins that share the enoyl-CoA hydratase/isomerase sequence motif. PubMed: 9739087DOI: 10.1016/S0969-2126(98)00098-7 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.5 Å) |
Structure validation
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