3E5H

Crystal Structure of Rab28 GTPase in the Active (GppNHp-bound) Form

Replaces:  2HY4

Summary for 3E5H

• Entry DOI: 10.2210/pdb3e5h/pdb
• Related: 2HXS
• Descriptor: Ras-related protein Rab-28, MAGNESIUM ION, PHOSPHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER, ... (5 entities in total)
• Functional Keywords: rab gtpase, signaling protein, cell membrane, gtp-binding, lipoprotein, membrane, nucleotide-binding, prenylation
• Biological source: Homo sapiens (human)
• Cellular location: Cell membrane ; Lipid-anchor ; Cytoplasmic side : P51157
• Total number of polymer chains: 1
• Total formula weight: 20711.66

Authors

Lee, S.H.,Baek, K.,Li, Y.,Dominguez, R. (deposition date: 2008-08-13, release date: 2008-08-26, Last modification date: 2023-08-30)

Primary citation

Lee, S.H.,Baek, K.,Dominguez, R.
Large nucleotide-dependent conformational change in Rab28.
Febs Lett., 582:4107-4111, 2008

PubMed Abstract: 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 1.1A 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.

PubMed: 19026641
DOI: 10.1016/j.febslet.2008.11.008

Experimental method

X-RAY DIFFRACTION (1.499 Å)