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. 2016 Jan 28;6:20007. doi: 10.1038/srep20007

Figure 2. GTPase domain mutants of SEPT7.

Figure 2

(A) Scheme for the organization of a septin hetero-oligomeric complex depicting the important interfaces of interaction. (B) Alignment of human H-Ras (NP_001123914), mouse Sept2 (NP_001153189) and SEPT7 (NP_001192296) sequences showing conserved regions in the GTPase domain- G1 box highlighted. (C) Sequence comparison of GTPase domain – switch I region residues in mouse SEPT7, SEPT2 and SEPT6 (NP_001170795.1). The conserved Threonine (T) residue critical for GTP binding and hydrolysis (in red) is absent in SEPT6 which makes it catalytically inactive. The critical residues selected for mutagenesis are in bold. (D) The structure of a homodimer of human SEPT7 bound to GDP (PDB 3T5D). The corresponding residues chosen for mutation in mouse SEPT7 are labeled and represented in the form of colored sticks [E202 in Chain A (magenta) and other sites indicated in chain B (green)] (Represented using PyMOL, loops in the structure were smoothened for a better representation). (E) Mutations introduced in SEPT7, expected outcomes and the scientific basis for the mutations tabulated.