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2Y8E

Crystal structure of D. melanogaster Rab6 GTPase bound to GMPPNP

Summary for 2Y8E
Entry DOI10.2210/pdb2y8e/pdb
DescriptorRAB-PROTEIN 6, SULFATE ION, PHOSPHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER, ... (5 entities in total)
Functional Keywordshydrolase, nucleotide binding, gtp binding
Biological sourceDROSOPHILA MELANOGASTER (FRUIT FLY)
Total number of polymer chains2
Total formula weight42067.26
Authors
Walden, M.,Edwards, T.A. (deposition date: 2011-02-04, release date: 2011-07-06, Last modification date: 2023-12-20)
Primary citationWalden, M.,Jenkins, H.T.,Edwards, T.A.
Structure of the Drosophila Melanogaster Rab6 Gtpase at 1.4 A Resolution
Acta Crystallogr.,Sect.F, 67:744-, 2011
Cited by
PubMed Abstract: Rab6 is a small GTPase that belongs to the p21 Ras superfamily. It is involved in vesicle trafficking between the Golgi apparatus and endosomes/ER in eukaryotes. The GDP-bound inactive protein undergoes conformational changes when the nucleotide is exchanged to GTP, allowing Rab6 to interact with a variety of different effector proteins. To further understand how these changes affect downstream protein binding, the crystal structure of Rab6 from Drosophila melanogaster has been solved to 1.4 Å resolution, the highest resolution for a Rab6 structure to date. The crystals belonged to space group C2, with unit-cell parameters a=116.5, b=42.71, c=86.86 Å, α=90, β=133.12, γ=90°. The model was refined to an R factor of 14.5% and an Rfree of 17.3%.
PubMed: 21795785
DOI: 10.1107/S1744309111017453
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.39 Å)
Structure validation

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數據於2024-11-06公開中

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