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 4
(a) Stereo figure showing the active site of M. fumariolicum SolV (shades of green) superimposed with that of E. coli DapA (light blue/grey). A sulfate (or phosphate; see text) ion is bound in the active site. The residues of the catalytic triad, as well as the catalytic lysine, superimpose closely. (b) Stereo figure showing the putative allosteric pocket in M. fumariolicum SolV (shades of green) superimposed with that in the lysine-inhibited C. jejuni DapA structure (dark red/brown). The residues interacting with the allosteric lysine (Lys) in the C. jejuni structure are conserved in M. fumariolicum SolV DapA, including His56, which is believed to be diagnostic for allosteric regulation. Residues from an adjacent subunit are marked with an apostrophe.

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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