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Figure 4
Analysis of a putative ATP/Mg2+-binding site in EccCDUF domains of ESX-1–ESX-5 systems from Mtb, Msm and Mxp. (a) Sequence alignment of the Walker A and B motifs (coloured blue and pink, respectively). (b) Structural details of the Walker A and B motifs observed in [Mtb{\rm EccC_5^{DUF}}] (crystal structure), [Mxp{\rm EccC_5^{DUF}}] (PDB entry 7b9s), [Msm{\rm EccC_3^{DUF}}] (PDB entry 6gsx), [Mtb{\rm EccC_1^{DUF}}] (AlphaFold model, UniProt entry P9WNB3), [Mtb{\rm EccC_2^{DUF}}] (AlphaFold model, UniProt entry O05450) and [Mtb{\rm EccC_4^{DUF}}] (AlphaFold model, UniProt entry P9WNA7) represented as cartoons and following the same colour code as in (a). Amino acids substituting key residues for ATP/Mg2+ interaction, or involved in hydrogen-bond/salt-bridge interactions, are depicted as sticks.

Journal logoSTRUCTURAL
BIOLOGY
ISSN: 2059-7983
Volume 80| Part 6| June 2024| Pages 397-409
https://doi.org/10.1107/S2059798324004248
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