Structural insights into the dual nucleotide exchange and GDI displacement activity of SidM/DrrA
| العنوان: | Structural insights into the dual nucleotide exchange and GDI displacement activity of SidM/DrrA |
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| المؤلفون: | Yeon Gil Kim, Dong Won Lee, Bonsu Ku, Sung Jin Choi, Jae Sung Woo, Hye Young Suh, Byung-Ha Oh, Kwang Hoon Lee |
| المصدر: | The EMBO Journal. 29:496-504 |
| بيانات النشر: | Wiley, 2009. |
| سنة النشر: | 2009 |
| مصطلحات موضوعية: | Models, Molecular, Protein Conformation, Molecular Sequence Data, GTPase, Plasma protein binding, Biology, Guanosine triphosphate, Guanosine Diphosphate, Article, General Biochemistry, Genetics and Molecular Biology, Legionella pneumophila, Substrate Specificity, chemistry.chemical_compound, Protein structure, Bacterial Proteins, Guanine Nucleotide Exchange Factors, Humans, Point Mutation, rho-Specific Guanine Nucleotide Dissociation Inhibitors, Magnesium, Amino Acid Sequence, Molecular Biology, Guanine Nucleotide Dissociation Inhibitors, General Immunology and Microbiology, General Neuroscience, fungi, RAB1, Cell biology, DNA-Binding Proteins, rab1 GTP-Binding Proteins, chemistry, Biochemistry, Guanosine diphosphate, Liposomes, embryonic structures, Guanosine Triphosphate, Guanine nucleotide exchange factor, Legionnaires' Disease, Sequence Alignment, Protein Binding |
| الوصف: | 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. |
| تدمد: | 1460-2075 0261-4189 |
| URL الوصول: | https://explore.openaire.eu/search/publication?articleId=doi_dedup___::22ea7ade433f311140521d2a0e9ee3d1 https://doi.org/10.1038/emboj.2009.347 |
| حقوق: | OPEN |
| رقم الأكسشن: | edsair.doi.dedup.....22ea7ade433f311140521d2a0e9ee3d1 |
| قاعدة البيانات: | OpenAIRE |
| تدمد: | 14602075 02614189 |
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