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5ZAI

Crystal structure of 3-Hydroxypropionyl-CoA dehydratase from Metallosphaera sedula

Summary for 5ZAI
Entry DOI10.2210/pdb5zai/pdb
Descriptor3-hydroxypropionyl-coenzyme A dehydratase, COENZYME A, 1,2-ETHANEDIOL, ... (5 entities in total)
Functional Keywordshydrolase
Biological sourceMetallosphaera sedula
Total number of polymer chains6
Total formula weight174791.00
Authors
Lee, D.,Kim, K.J. (deposition date: 2018-02-07, release date: 2018-08-01, Last modification date: 2023-11-22)
Primary citationLee, 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: 30013155
DOI: 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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