Table 1.
Overview of identified cross-linked peptides.
| Protein(s) | Linked Residues | A Peptide | B Peptide | (Å) | ZapA, No Ca2+ | No ZapA, Ca2+ | ||
|---|---|---|---|---|---|---|---|---|
| Spectral Counts b | Type | Spectral Counts | Type | |||||
| FtsZ | 141–66 | KR | TAVGQTIQIGSGITKGLGAGANPEVGR | 24.8 | 11 | Intra | 6 | Intra |
| FtsZ | 141–133 | KR | DLGILTVAVVTKPFNFEGK | 12.3 | 2 | Intra | – | – |
| FtsZ-FtsZ | 141–367 | KR | VVNDNAPQTAKEPDYLDIPAFLR | u | 3 | Intra | 4 | Intra |
| FtsZ-FtsZ | 141–380 | KR | KQAD | u | 3 | Intra | 9 | Mix |
| FtsZ-FtsZ | 170–367 | LLKVLGR | VVNDNAPQTAKEPDYLDIPAFLR | u | - | - | 3 | Mix |
| FtsZ-FtsZ | 380–51 | KQAD | KTAVGQTIQIGSGITK | u | 5 | Intra | 13 | Mix |
| FtsZ | 380–66 | KQAD | TAVGQTIQIGSGITKGLGAGANPEVGR | u | 4 | Intra | - | - |
| FtsZ-FtsZ | 380–170 | KQAD | LLKVLGR | u | 3 | Intra | 5 | Mix |
| FtsZ-FtsZ | 380–367 | KQAD | VVNDNAPQTAKEPDYLDIPAFLR | u | 5 | Intra | 10 | Intra |
| ZapA-FtsZ | 42–51 | LQDLKER | KTAVGQTIQIGSGITK | 15.4 a | 5 | Inter | ||
| ZapA-FtsZ | 42–66 | LQDLKER | TAVGQTIQIGSGITKGLGAGANPEVGR | 16.8 a | 4 | Inter | ||
| ZapA-ZapA | 42–42 | LQDLKER | LQDLKER | 26.3 | 2 | Inter | ||
| ZapA-ZapA | 42–103 | LQDLKER | ITEKTNQNFE | 23.9 | 3 | Inter | ||
| ZapA-ZapA | 71–103 | AKTR | ITEKTNQNFE | 8.4 | 8 | Inter | ||
| ZapA-ZapA | 71–69 | AKTR | VTNEQLVFIAALNISYELAQEKAK | 9.0 | 2 | Inter | ||
| ZapA-ZapA | 103–103 | ITEKTNQNFE | ITEKTNQNFE | 22.3 | 1 | Inter |
Intra, intraprotein cross-link; inter, interprotein cross-link; u, cross-link with the unstructured C-terminal tail. Linked residues are in bold font. a Distances are based on the HADDOCK model of ZapA and FtsZ as shown in Figure 7. b Spectral counts, number of times that the precursor was selected in data-dependent acquisition leading to identification of the cross-linked peptide.