Structural Insights into the Mechanism of Dynamin Superfamily Proteins - PubMed (original) (raw)

Figure 3.. Biochemical and Structural Features of the GTPase Domain from Dynamin Superfamily Proteins (DSPs).

(A) Nucleotide-binding and hydrolysis motifs are conserved in all DSPs and small GTPases (e.g., HRas). Protein accession codes are as follows: dynamin 1 (GenBank: AAH50279.2), Drp1 (NCBI reference sequence: NP_001317309.1), OPA1 (GenBank: AKI72360.1), mitofusin 1 (GenBank: EAW78406.1), atlastin 1 (GenBank: AAH10708.2), GBP1 (NCBI reference sequence: NP_002044.2), MxA (NCBI reference sequence: NP_001171517.1), Vps1p (UniProtKB: P21576.2), Dnm1p (GenBank: CAA97444.1), Mgm1p (GenBank: ONH78423.1), Fzo1p (GenBank: EWH19560.1), Sey1p (GenBank: AJU15101.1), BDLP (UniProKB: B2IZD3.1), DynA (GenBank: CAB14120.1), and HRas (GenBank: AAH99130.1). Biochemical properties of dynamin GTPases depicting the guanine nucleotide kcat and binding affinities (right columns) for dynamin GTPases compared with the small GTPase, HRas. (Dynamin 1 [,–162], Drp1 [32,116,118,163,164], OPA1 [165], Mitofusin 1 [34,35], Atlastin 1 [46,133], GBP1 [36,166], MxA [167], Vps1p [168], Dnm1p [169,170], Mgm1p [171], Fzo1p, Sey1p [127], BDLP [26], DynA, and HRas [172,173]). (B) Nucleotide-mediated dimerization of the GTPase domain of dynamin with a bound GDP/AlF4− (orange) [Protein Data Bank (PDB): 2X2E] [43]. (C) Structure of the nucleotide-binding pocket illustrating conserved motifs. GTPase domain dimerization is stabilized via trans stabilizing residues (e.g., D180) that promote nucleotide binding and hydrolysis [43]. Motifs color-coded as in (A).