5ZAI
Crystal structure of 3-Hydroxypropionyl-CoA dehydratase from Metallosphaera sedula
Summary for 5ZAI
| Entry DOI | 10.2210/pdb5zai/pdb |
| Descriptor | 3-hydroxypropionyl-coenzyme A dehydratase, COENZYME A, 1,2-ETHANEDIOL, ... (5 entities in total) |
| Functional Keywords | hydrolase |
| Biological source | Metallosphaera sedula |
| Total number of polymer chains | 6 |
| Total formula weight | 174791.00 |
| Authors | |
| Primary citation | Lee, D.,Kim, K.J. Structural Insight into Substrate Specificity of 3-Hydroxypropionyl-Coenzyme A Dehydratase from Metallosphaera sedula Sci Rep, 8:10692-10692, 2018 Cited by PubMed Abstract: Metallosphaera sedula is a thermoacidophilic autotrophic archaeon known to utilize the 3-hydroxypropionate/4-hydroxybutyrate cycle (3-HP/4-HB cycle) as carbon fixation pathway. 3-Hydroxypropionyl-CoA dehydratase (3HPCD) is an enzyme involved in the 3-HP/4-HB cycle by converting 3-hydroxypropionyl-CoA to acryloyl-CoA. To elucidate the molecular mechanism of 3HPCD from M. sedula (Ms3HPCD), we determined its crystal structure in complex with Coenzyme A (CoA). Ms3HPCD showed an overall structure and the CoA-binding mode similar to other enoyl-CoA hydratase (ECH) family enzymes. However, compared with the other ECHs, Ms3HPCD has a tightly formed α3 helix near the active site, and bulky aromatic residues are located at the enoyl-group binding site, resulting in the enzyme having an optimal substrate binding site for accepting short-chain 3-hydroxyacyl-CoA as a substrate. Moreover, based on the phylogenetic tree analysis, we propose that the 3HPCD homologues from the phylum Crenarchaeota have an enoyl-group binding pocket similar to that of bacterial short-chain ECHs. PubMed: 30013155DOI: 10.1038/s41598-018-29070-w PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.8 Å) |
Structure validation
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