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TitleStructures of mycobacterial 3-methylcrotonyl-CoA carboxylase reveal carrier-domain translocation between catalytic sites.
Journal, issue, pagesFEBS Lett, Year 2026
Publish dateSep 11, 2026
AuthorsAjit Yadav / Bogdan I Florea / Sebastian Geibel /
PubMed Abstract3-Methylcrotonyl-CoA carboxylase (MCC) catalyzes an essential step in leucine degradation. Here, we report two high-resolution cryo-EM structures of endogenous, biotin-bound Mycobacterium smegmatis ...3-Methylcrotonyl-CoA carboxylase (MCC) catalyzes an essential step in leucine degradation. Here, we report two high-resolution cryo-EM structures of endogenous, biotin-bound Mycobacterium smegmatis AccA1-AccD1 MCC. The αβ complex adopts a canonical architecture with a hexameric carboxyltransferase core flanked by trimeric biotin carboxylase modules. The structures capture BCCP engaged at either the BC or CT active site, revealing long-range carrier-domain translocation. In the CT-engaged state, local BC-domain shifts disrupt the BC-site BCCP-interaction network, disfavoring BCCP rebinding. Unlike human MCC, no comparable CT-core remodeling is observed, suggesting distinct mechanisms of carrier-domain coordination.
External linksFEBS Lett / PubMed:42723463
MethodsEM (single particle)
Resolution2.6 - 3.15 Å
Structure data

57132

29ex

EMDB-57132, PDB-29ex:
Cryo-EM structure of 3-methylcrotonyl- CoA carboxylase (MCC) complex (BC-engage BCCP state) from Mycobacterium smegmatis
Method: EM (single particle) / Resolution: 2.9 Å

57153

29gv

EMDB-57153, PDB-29gv:
Cryo-EM structure of 3-methylcrotonyl-CoA carboxylase (MCC) complex (CT-engaged BCCP state) from Mycobacterium smegmatis
Method: EM (single particle) / Resolution: 2.6 Å

58684

31vx

EMDB-58684, PDB-31vx:
Cryo-EM structure of 3-methylcrotonyl-CoA carboxylase (MCC) complex (BC-engaged BCCP state)from Mycobacterium smegmatis
Method: EM (single particle) / Resolution: 3.15 Å

Chemicals

ChemComp-BTN:
BIOTIN

Source
  • mycolicibacterium smegmatis mc2 155 (bacteria)
KeywordsLIGASE / Biotin carboxyalse

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