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1DCI

DIENOYL-COA ISOMERASE

Summary for 1DCI
Entry DOI10.2210/pdb1dci/pdb
DescriptorDIENOYL-COA ISOMERASE, SULFATE ION, MAGNESIUM ION, ... (5 entities in total)
Functional Keywordslyase, dienoyl-coa isomerase
Biological sourceRattus norvegicus (Norway rat)
Cellular locationMitochondrion: Q62651
Total number of polymer chains3
Total formula weight92548.37
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 citationModis, 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: 9739087
DOI: 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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