CryoEM structures reveal allosteric regulation of the catalytic activity of the multi-protein human MAT enzyme complexes

Khaja, F.T.; Vara, R.; Aspinall, L.P.; Merriman, C.; Maerivoet, A.; White, J.B.R.; Muench, S.P.; Hasnain, S.S.; Antonyuk, S.V.

doi:10.1107/S2052252526005075

Figure 5
Key structural insights into control, regulation and allosteric mechanism of MAT enzyme complexes. Chain-specific structural superposition of the MATα2 protomer in apo MATα2₄ (PDB ID: 6faj, Chain B), the SAMe + PPNP-bound MATα2₄βV2₂ complex (PDB ID: 4ndn, Chain B), and the resting-state cryoEM structures of MATα2₄βV2₂ (Chain B) and MATα2₄βV1₂ (Chain B) illustrates allosteric conformational changes near the active-site pocket upon MATβV binding. The right inset presents an expanded stick view of the active-site pocket, highlighting the spatial orientation of key residues and showing how MATβV modulates the architecture of the MATα2 active site. The MATα2 protomers used as references for chain-specific structural superposition are indicated with asterisks, and all structures are colour-coded as indicated.

IUCrJ

Volume 13| Part 4| July 2026|

ISSN: 2052-2525

https://doi.org/10.1107/S2052252526005075

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