Extended Data Fig. 8: The conserved Tyr-VIa residue BAK1 Y403 is in close proximity to the catalytic loop and to C408. | Nature

Extended Data Fig. 8: The conserved Tyr-VIa residue BAK1 Y403 is in close proximity to the catalytic loop and to C408.

From: Phosphocode-dependent functional dichotomy of a common co-receptor in plant signalling

Extended Data Fig. 8

a, In silico representation of the structure of BAK1CD (PDB ID: 3UIM). The activation-segment region is shown in green and the catalytic loop in purple. b, Conservation of BAK1 Y403 in SERK proteins across plant species. Clustal Omega multiple alignments were visualized using JalView v2.10.2b2. The alignment is coloured by percentage identity. Magenta, conservation of BAK1 Y403. Protein IDs used for the alignments are as follows: PpSERK1(B9MW41), PpSERK2(B9IQM9), PpSERK3(B9HFX1), PpSERK4(B9H599), DlSERK(B5TTV0), MtSERK1(Q8GRK2), MtSERK2(E2IXG1), MtSERK3(E2IXG8), MtSERK4(E2IXG2), MtSERK5(E2IXG3), MtSERK6(E2IXG4), GmSERK1(C6ZGA8), GmSERK2(C6FF61), CuSERK (Q6BE26), CsSERK(C3V9W0), VvSERK1(D7TXV2), VvSERK2(A5BIY4), VvSERK3(D7STF6), CpSERK1(A7L5U3), CpSERK2(E5D6S9), GhSERK1(E5Q8K6), GhSERK2(F5BZU9), GhSERK3(F6MF11), StSERK(A3R789), SpSERK(A6N8J2), SlSERK1(G0XZA3), SlSERK3A(G0XZA5), SlSERK3B(G0XZA6), DcSERK(O23921), AtSERK1(Q94AG2), AtSERK2(Q9XIC7), AtSERK3(Q94F62), AtSERK4(Q9SKG5), AtSERK5(Q8LPS5), NbSERK3A(E3VXE6), NbSERK3B(E3VXE7), OsbiSERK(Q6S7F1), OsSERK(Q5Y8C8), OsSERKlike1(Q67X31), OsSERKlike2(Q6K4T4), SbSERK1(C5YHV3), SbSERK2(C5Y9S6), SbSERK3(C5XVP5), AcSERK1(H6SU43), AcSERK2(H6UP78), AcSERK3(H6UP79), ClSERK(G2XLB1), CnSERK(Q5S1N9), ZmSERK1(Q93W70), ZmSERK2(Q94IJ5), ZmSERK3(B4G007), TaSERK1(G4XGX1), TaSERK2(G4XGX2), TaSERKlike3(G4XGX3), SmSERK1(D8SBB8), SmSERK2(D8S0N3), SmSERK3(D8S4M4), SmSERK4(D8R6C9), MpSERK(A7VM18), PpSERK1(A9STU8), PpSERK2(A9SMW5), PpSERK3(A9RY79), PoapSERKlike1(Q659J0), PoapSERKlike2(Q659J1), CeSERK(A7VM46).

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