Large nucleotide-dependent conformational change in Rab28

• Published in: FEBS letters Vol. 582; no. 29; pp. 4107 - 4111
• Main Authors: Lee, Sung Haeng, Baek, Kyuwon, Dominguez, Roberto
• Format: Journal Article
• Language: English
• Published: England Elsevier B.V 10.12.2008
• Subjects: Amino Acid Sequence; CONFORMATIONAL CHANGES; CRYSTAL STRUCTURE; Crystallography, X-Ray; FLEXIBILITY; GDP-3′P; GTP analog GppNHp; GTP-ASES; Guanosine Diphosphate - chemistry; Guanylyl Imidodiphosphate - chemistry; Humans; MATERIALS SCIENCE; MEMBRANES; Protein Conformation; rab GTP-Binding Proteins - chemistry; Rab GTPase family; RESOLUTION; Rab GTPase family; GDP-3′P; GTP analog GppNHp; Crystal structure
• ISSN: 0014-5793; 1873-3468
• DOI: 10.1016/j.febslet.2008.11.008

Rab GTPases are essential regulators of membrane trafficking. We report crystal structures of Rab28 in the active (GppNHp-bound) and inactive (GDP-3′P-bound) forms at 1.5 and 1.1 Å resolution. Rab28 is a distant member of the Rab family. While the overall fold of Rab28 resembles that of other Rab GTPases, it undergoes a larger nucleotide-dependent conformational change than other members of this family. Added flexibility resulting from a double-glycine motif at the beginning of switch 2 might partially account for this observation. The double-glycine motif, which is conserved in the Arf family, only occurs in Rab28 and Rab7B of the Rab family, and may have a profound effect on their catalytic activities.