Large nucleotide-dependent conformational change in Rab28 |
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Authors: | Sung Haeng Lee Kyuwon Baek |
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Institution: | a Department of Physiology, University of Pennsylvania School of Medicine, 3700 Hamilton Walk, A507 Richards Building, Philadelphia, PA 19104-6085, USA b Chosun University School of Medicine, Department of Cellular and Molecular Medicine, Gwangju, Korea |
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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 1.1 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. |
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Keywords: | Crystal structure GDP-3&prime P GTP analog GppNHp Rab GTPase family |
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