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4J0E

Crystal structure of 3-hydroxyacyl-CoA dehydrogenase from Caenorhadbitis elegans in P1 space group

Summary for 4J0E
Entry DOI10.2210/pdb4j0e/pdb
Related4J0F
DescriptorProbable 3-hydroxyacyl-CoA dehydrogenase F54C8.1 (2 entities in total)
Functional Keywordsrossmann fold, dehydrogenase, fatty acid beta-oxidation, nadh binding, mitochondrial matrix, oxidoreductase
Biological sourceCaenorhabditis elegans (nematode)
Cellular locationMitochondrion matrix : P34439
Total number of polymer chains2
Total formula weight69419.45
Authors
Xu, Y.,Sun, F.,Zhai, Y. (deposition date: 2013-01-30, release date: 2014-03-19, Last modification date: 2023-11-08)
Primary citationXu, Y.,Sun, F.
Purification, crystallization and preliminary crystallographic analysis of 3-hydroxyacyl-CoA dehydrogenase from Caenorhabditis elegans.
Acta Crystallogr.,Sect.F, 69:515-519, 2013
Cited by
PubMed Abstract: 3-Hydroxyacyl-CoA dehydrogenase (HAD; EC 1.1.1.35) is the enzyme that catalyzes the third step in fatty-acid β-oxidation, oxidizing the hydroxyl group of 3-hydroxyacyl-CoA to a keto group. The 3-hydroxyacyl-CoA dehydrogenase from Caenorhabditis elegans (cHAD) was cloned, overexpressed in Escherichia coli and purified to homogeneity for crystallography. Initial crystals were obtained by the hanging-drop vapour-diffusion method. Optimization of the precipitant concentration and the pH yielded two types of well diffracting crystals with parallelepiped and cuboid shapes, respectively. Complete diffraction data sets were collected and processed from both crystal types. Preliminary crystallographic analysis indicated that the parallelepiped-shaped crystal belonged to space group P1, while the cuboid-shaped crystal belonged to space group P212121. Analyses of computed Matthews coefficient and self-rotation functions suggested that there are two cHAD molecules in one asymmetric unit in both crystals, forming identical dimers but packing in distinct manners.
PubMed: 23695566
DOI: 10.1107/S1744309113007045
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.6 Å)
Structure validation

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