Structure of the 4-hydroxy-tetrahydrodipicolinate synthase from the thermoacidophilic methanotroph Methylacidiphilum fumariolicum SolV and the phylogeny of the aminotransferase pathway

Schmitz, R.A.; Dietl, A.; Müller, M.; Berben, T.; Op den Camp, H.J.M.; Barends, T.R.M.

doi:10.1107/S2053230X20005294

Acta Crystallographica Section F
Acta Crystallographica
Section F STRUCTURAL BIOLOGY COMMUNICATIONS

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Figure 5
Superposition of DapA from M. fumariolicum SolV (SolV, green) with DapA from C. jejuni without (C. jejuni, blue) and with (C. jejuni + Lys, red) lysine in the allosteric pocket. The protein is shown as a cartoon; the covalent adduct in the active site (Act.) and the lysine in the allosteric pocket (All.) are shown as sticks. The approximate boundary between the domains is indicated by the dashed line. Domain 1 of the C. jejuni structure was used for superposition. Domain 2 of the SolV protein superimposes closely with the corresponding domain in the C. jejuni protein without lysine in the allosteric site and less well with the structure of the C. jejuni enzyme with a lysine bound in the allosteric pocket.

STRUCTURAL BIOLOGY
COMMUNICATIONS

ISSN: 2053-230X

Volume 76| Part 5| May 2020| Pages 199-208

https://doi.org/10.1107/S2053230X20005294

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