5zai | pdb_00005zai
Crystal structure of 3-Hydroxypropionyl-CoA dehydratase from Metallosphaera sedula
Structural highlights
Function[HPCD_METS5] Plays a role in autotrophic carbon fixation via the 3-hydroxypropionate/4-hydroxybutyrate cycle. Catalyzes the reversible dehydration of 3-hydroxypropionyl-CoA to form acryloyl-CoA, and the reversible dehydration of (S)-3-hydroxybutyryl-CoA to form crotonyl-CoA. Inactive towards (R)-3-hydroxybutyryl-CoA.[1] Publication Abstract from PubMedMetallosphaera 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 alpha3 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. Structural Insight into Substrate Specificity of 3-Hydroxypropionyl-Coenzyme A Dehydratase from Metallosphaera sedula.,Lee D, Kim KJ Sci Rep. 2018 Jul 16;8(1):10692. doi: 10.1038/s41598-018-29070-w. PMID:30013155[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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