| Primary Identifier | IPR030381 | Type | Domain |
| Short Name | G_DYNAMIN_dom |
| description | This entry represents the dynamin-type guanine nucleotide-binding (G) domain. Members of the dynamin GTPase family appear to be ubiquitous. They catalyze diverse membrane remodelling events in endocytosis, cell division, and plastid maintenance. Their functional versatility also extends to other core cellular processes, such as maintenance of cell shape or centrosome cohesion. Members of the dynamin family are characterised by their common structure and by conserved sequences in the GTP-binding domain. The minimal distinguishing architectural features that are common to all dynamins and are distinct from other GTPases are the structure of the large GTPase domain (~280 amino acids) and the presence of two additional domains: the middle domain and the GTPase effector domain (GED), which are involved in oligomerization and regulation of the GTPase activity. In many dynamin family members, the basic set of domains is supplemented by targeting domains, such as: pleckstrin-homology (PH) domain, proline-rich domains (PRDs), or by sequences that target dynamins to specific organelles, such as mitochondria and chloroplasts [, , ]. The dynamin-type G domain consists of a central eight-stranded β-sheetsurrounded by seven alpha helices and two one-turn helices.It contains the five canonical guanine nucleotide binding motifs (G1-5). TheP-loop (G1) motif (GxxxxGKS/T) is also present in ATPases (Walker A motif) andfunctions as a coordinator of the phosphate groups of the bound nucleotide. Aconserved threonine in switch-I (G2) and the conserved residues DxxG ofswitch-II (G3) are involved in Mg(2+) binding and GTP hydrolysis. Thenucleotide binding affinity of dynamins is typically low, with specificity forGTP provided by the mostly conserved N/TKxD motif (G4). The G5 or G-cap motifis involved in binding the ribose moiety [, , ].Some proteins containing a dynamin-type G domain are listed below [, ]:Animal dynamin, the prototype for this family. The role of dynamin inendocytosis is well established. Additional roles were proposed in vesiclebudding from the trans-Golgi network (TGN) and the budding of caveolae fromthe plasma membrane [].Vetebrate Mx proteins, a group of interferon (IFN)-induced GTPases involvedin the control of intracellular pathogens [, ].Eukaryotic Drp1 (Dnm1 in yeast) mediates mitochondrial and peroxisomalfission.Eukaryotic Eps15 homology (EH)-domain-containing proteins (EHDs), ATPasesimplicated in clathrin-independent endocytosis and recycling fromendosomes. The dynamin-type G domains of EHDs bind to adenine rather thanto guanine nucleotide [, ].Yeast to human OPA1/Mgm1 proteins. They are found between the inner andouter mitochondrial membranes and are involved in mitochondrial fusion.Yeast to human mitofusin/fuzzy onions 1 (Fzo1) proteins, involved inmitochondrial dynamics [, ].Yeast vacuolar protein sorting-associated protein 1 (Vps1), involved invesicle trafficking from the Golgi.Escherichia coli clamp-binding protein CrfC (or Yjda), important for thecolocalization of sister nascent DNA strands after replication fork passageduring DNA replication, and for positioning and subsequent partitioning ofsister chromosomes [].Nostoc punctiforme bacterial dynamin-like protein (BDLP) [, ]. |
