The structure of succinyl-CoA synthetase bound to the succinyl-phosphate intermediate clarifies the catalytic mechanism of ATP-citrate lyase

Huang, J.; Fraser, M.E.

doi:10.1107/S2053230X22008810

Acta Crystallographica Section F
Acta Crystallographica
Section F STRUCTURAL BIOLOGY COMMUNICATIONS

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Figure 4
The structure of succinyl-CoA synthetase bound to the succinyl-phosphate intermediate clarifies the catalytic mechanism of ATP-citrate lyase. C atoms are yellow and purple for the succinyl-phosphate complex, green for the wild type with succinate and phosphate, and cyan for the mutant with succinate and phosphate. Water molecules are red for the succinyl-phosphate complex, pink for the wild type and grey for the mutant with succinate and phosphate. Other atoms are coloured according to type. Distances from the side-chain carbonyl O atom of Gln105α to the magnesium ion and from the carboxylate O atom of Glu105α to the water molecules are shown in Å.

STRUCTURAL BIOLOGY
COMMUNICATIONS

ISSN: 2053-230X

Volume 78| Part 10| October 2022| Pages 363-370

https://doi.org/10.1107/S2053230X22008810

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