Structures of Listeria monocytogenes MenD in ThDP-bound and in-crystallo captured intermediate I-bound forms

Bailey, M.; Given, F.M.; Ho, N.A.T.; Pearce, F.G.; Allison, T.M.; Johnston, J.M.

doi:10.1107/S2053230X25006181

Acta Crystallographica Section F
Acta Crystallographica
Section F STRUCTURAL BIOLOGY COMMUNICATIONS

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Figure 4
(a) Overlay of the putative LmoMenD (PDB entry 9e9b; green) and MtbMenD (PDB entry 6o0j; grey) DHNA (orange) binding sites. Residues hypothesized to fulfil equivalent functions to a particular M. tuberculosis arginine-cage constituent are in bold, with LmoMenD Lys325 potentially able to fulfil the function of MtbMenD Arg277 or Arg303. (b) Surface representation of the MtbMenD (PDB entry 6o0j; grey) allosteric site showing the DHNA (orange) binding pocket. (c) Surface representation of the LmoMenD (PDB entry 9mnn; green) putative allosteric site, highlighting the requirement of induced-fit conformational changes to accommodate DHNA (orange) binding.

STRUCTURAL BIOLOGY
COMMUNICATIONS

ISSN: 2053-230X

Volume 81| Part 8| August 2025| Pages 348-357

https://doi.org/10.1107/S2053230X25006181

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