5xc3

Crystal structure of Acanthamoeba polyphaga mimivirus Rab GTPase in complex with GDP

spinqualitylabelsall models 5xc3, resolution 1.50Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5xc3 is a 1 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: GDP, MG Related: 5xc5 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [RABL_MIMIV] May be involved in protein transport. Publication Abstract from PubMed Acanthamoeba polyphaga mimivirus (APMV) is a member of the family of giant viruses, harboring a 1,200 kbp genome within its 700 nm-diameter viral particle. The R214 gene of the APMV genome was recently shown to encode a homologue of the Rab GTPases, molecular switch proteins known to play a pivotal role in the regulation of membrane trafficking that were considered to exist only in eukaryotes. Herein, we report the first crystal structures of GDP- and GTP-bound forms of APMV Rab GTPase, both of which were determined at high resolution. An in-depth structural comparison of APMV Rab with each other and with mammalian Rab homologues led to an atomic-level elucidation of the inactive-active conformational change upon GDP/GTP exchange. APMV Rab GTPase exhibited considerable structural similarity to human Rab5, as previously predicted based on its amino acid sequence. However, it also contains unique structural features differentiating it from mammalian homologues, such as the functional substitution of a phenylalanine residue for the stabilization of the nucleotide's guanine base. Crystal structures of two forms of the Acanthamoeba polyphaga mimivirus Rab GTPase.,Ku B, You JA, Oh KJ, Yun HY, Lee HS, Shin HC, Jung J, Shin YB, Kim SJ Arch Virol. 2017 Nov;162(11):3407-3416. doi: 10.1007/s00705-017-3510-2. Epub 2017, Aug 4. PMID:28779233 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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