A Novel Unorthodox Dimeric Primary Enoyl-CoA Reductase Structure.

ABSTRACT: Enoyl-CoA carboxylases/reductases (ECRs) are enzymes with the fastest carbon dioxide (CO₂) fixation capabilities, yet the precise mechanisms behind their assembly and catalytic activity are structurally not yet fully understood. Here, we employed cryo X-ray crystallography to reveal the dimeric structural organization of a novel ECR, isolated from mesophilic Mesorhizobium metallidurans (M. metallidurans). We examined the interactions in silico and compared oligomerization of our dimeric ECR from M. metallidurans (ECR^Mm_Dim) with tetrameric ECR from Burkholderia ambifaria (ECR^Ba_Tet)by using size exclusion chromatography in solution. Our in silico analysis revealed that specific residues in the M. metallidurans

SUBMITTER: Kulakman C 

PROVIDER: S-EPMC12632816 | biostudies-literature | 2025 Oct

REPOSITORIES: biostudies-literature