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Structural insights into the dual nucleotide exchange and GDI displacement activity of SidM/DrrA.

Suh HY, Lee DW, Lee KH, Ku B, Choi SJ, Woo JS, Kim YG, Oh BH
EMBO J 29 496-504 (2010)
Cited: 51 times
EuropePMC logo PMID: 19942850

Abstract

GDP-bound prenylated Rabs, sequestered by GDI (GDP dissociation inhibitor) in the cytosol, are delivered to destined sub-cellular compartment and subsequently activated by GEFs (guanine nucleotide exchange factors) catalysing GDP-to-GTP exchange. The dissociation of GDI from Rabs is believed to require a GDF (GDI displacement factor). Only two RabGDFs, human PRA-1 and Legionella pneumophila SidM/DrrA, have been identified so far and the molecular mechanism of GDF is elusive. Here, we present the structure of a SidM/DrrA fragment possessing dual GEF and GDF activity in complex with Rab1. SidM/DrrA reconfigures the Switch regions of the GTPase domain of Rab1, as eukaryotic GEFs do toward cognate Rabs. Structure-based mutational analyses show that the surface of SidM/DrrA, catalysing nucleotide exchange, is involved in GDI1 displacement from prenylated Rab1:GDP. In comparison with an eukaryotic GEF TRAPP I, this bacterial GEF/GDF exhibits high binding affinity for Rab1 with GDP retained at the active site, which appears as the key feature for the GDF activity of the protein.

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  2. Allosteric binding sites in Rab11 for potential drug candidates. Kumar AP, Lukman S. PLoS ONE 13 e0198632 (2018)


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  7. The Mon1-Ccz1 GEF activates the Rab7 GTPase Ypt7 via a longin-fold-Rab interface and association with PI3P-positive membranes. Cabrera M, Nordmann M, Perz A, Schmedt D, Gerondopoulos A, Barr F, Piehler J, Engelbrecht-Vandré S, Ungermann C. J. Cell. Sci. 127 1043-1051 (2014)
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  16. Structural analyses of Legionella LepB reveal a new GAP fold that catalytically mimics eukaryotic RasGAP. Yu Q, Hu L, Yao Q, Zhu Y, Dong N, Wang DC, Shao F. Cell Res. 23 775-787 (2013)
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  20. Innate immunity kinase TAK1 phosphorylates Rab1 on a hotspot for posttranslational modifications by host and pathogen. Levin RS, Hertz NT, Burlingame AL, Shokat KM, Mukherjee S. Proc. Natl. Acad. Sci. U.S.A. 113 E4776-83 (2016)
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  22. Lpg0393 of Legionella pneumophila is a guanine-nucleotide exchange factor for Rab5, Rab21 and Rab22. Sohn YS, Shin HC, Park WS, Ge J, Kim CH, Lee BL, Heo WD, Jung JU, Rigden DJ, Oh BH. PLoS ONE 10 e0118683 (2015)
  23. A guanine nucleotide exchange factor (GEF) limits Rab GTPase-driven membrane fusion. Langemeyer L, Perz A, Kümmel D, Ungermann C. J. Biol. Chem. 293 731-739 (2018)
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  26. Legionella- and host-driven lipid flux at LCV-ER membrane contact sites promotes vacuole remodeling. Vormittag S, Hüsler D, Haneburger I, Kroniger T, Anand A, Prantl M, Barisch C, Maaß S, Becher D, Letourneur F, Hilbi H. EMBO Rep 24 e56007 (2023)
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