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    QatB–QatC: essential mutations & structural features (from manuscript data)

    Extracted only from the provided paper records (structural biology + in vivo mutagenesis) for the two manuscripts: and .
    Epistemic note: “Essential” here means reduced/abolished anti-phage defense in the reported functional assays (not absolute biochemical indispensability). The exact catalytic chemistry/substrate remains unresolved in these records.

    Mutation classes with functional impact (from listed tested variants)

    Table A — QatC essential mutations & structural features

    QatC feature Residues / motif (as reported) Structural context (as reported) Mutation(s) tested Functional effect on anti-phage defense (as reported) Evidence source(s)
    ATP/catalytic motif (pyrophosphate-binding region) S156; D160; S161 Conserved catalytic region in QatC; ATP-bound QatB–QatC structure links these residues to nucleotide binding/interactions S156A; S161A; S156A/S161A Reported to be important: catalytic-residue mutations reduce/impair anti-phage function
    Zinc coordination (catalytic-core requirement) C332; C352; C355; C358 QatC QueC-like core coordinates Zn2+; mutations of these cysteines disrupt activity Zinc-coordinating cysteine mutations (specific identities not fully enumerated in the provided record) Reported to reduce anti-phage activity; supports catalytic role of QatC zinc center
    Interface/contact residues important for complex integrity Examples reported: A404, P422, F282, L269, P268, F415 (with QatB hydrophobic contacts); R454/R412 with QatB acidic residues (D212/D166/E162) Large QatB–QatC interface within QatC N- and C-terminal extensions; multiple contact types (hydrophobic + salt bridges) Interface/contact mutational analysis described as reducing complex formation and activity (exact interface mutation list not fully enumerated in the provided record) Reported to reduce complex formation/anti-phage activity; supports essential interfacial architecture

    Table B — QatB essential mutations & structural features in QatB–QatC

    QatB feature Residues / motif (as reported) Structural context (as reported) Mutation(s) tested Functional effect on anti-phage defense (as reported) Evidence source(s)
    N-terminal MGTS motif (including critical G2) MGTS; with G2 explicitly tested as G2D QatB N-terminal tail/loop inserts into QatC active-site region and is required for anti-phage activity G2D; N-terminal motif perturbations (MGTS-related) Reported to disrupt defense when mutated (G2D impairs anti-phage function)
    Deletion of a specific N-terminal segment (critical window) Residues 16–22 (as deletion tested: Δ16–22) Implicates a critical N-terminal segment for proper insertion/contacting QatC catalytic center Δ16–22 Reported to disrupt defense
    Deletion of downstream N-terminal segment (non-critical window in this report) Residues 34–40 (as deletion tested: Δ34–40) Suggests positional/structural specificity within the N-terminus for QatC engagement Δ34–40 Reported to not disrupt defense (in the first record’s described outcomes)
    Additional N-terminal deletion/mutation patterns (beyond first record) Examples explicitly mentioned: Δ14–20; M1 processing effects Further supports that precise N-terminus geometry/processing is required for engagement with QatC catalytic center Δ14–20; processing-related perturbations (M1 processing; exact notation summarized) Reported to impair anti-phage activity

    QatB vs QatC: “what’s emphasized” structurally in the provided manuscript records

    Confidence, limitations, and what could change these tables

    • Not all mutations are exhaustively enumerated: the tables reflect only the mutations/residue sets explicitly present in the provided manuscript records (e.g., specific zinc-cysteine mutation identities are not fully enumerated in the record, though zinc residues themselves are).
    • Catalytic chemistry remains unresolved: both records indicate that the exact substrate and reaction remain to be determined (including lack of conclusive detectable CDG-dependent ATP pyrophosphatase activity under tested conditions in the second record).
    • Structural-state ambiguity: the ATP-bound structure is described without CDG density in the provided record, so binding events do not necessarily prove downstream chemistry.
    • Discrepancies between records may reflect different residue numbering conventions: the zinc-coordination cysteine identifiers show differently (C332/C352/C355/C358 vs C334/C354/C357/C360) across the two provided manuscripts’ excerpts. This could be true biological difference, alignment/numbering convention differences, or reporting summarization; verifying against the PDB residue maps would be needed.


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    Updated: May 01, 2026

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