2y44

Crystal structure of GARP from Trypanosoma congolense

spinqualitylabelsall models 2y44, resolution 1.65Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2y44 is a 1 chain structure with sequence from Trypanosoma congolense. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.65Å Ligands: GOL, IOD, OCS Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function Q07419_TRYCO Publication Abstract from PubMed Trypanosoma congolense is an African trypanosome that causes serious disease in cattle in Sub-Saharan Africa. The four major life cycle stages of T. congolense can be grown in vitro, which has led to the identification of several cell-surface molecules expressed on the parasite during its transit through the tsetse vector. One of these, glutamic acid/alanine-rich protein (GARP), is the first expressed on procyclic forms in the tsetse midgut and is of particular interest because it replaces the major surface coat molecule of bloodstream forms, the variant surface glycoprotein (VSG) that protects the parasite membrane, and is involved in antigenic variation. Unlike VSG, however, the function of GARP is not known, which necessarily limits our understanding of parasite survival in the tsetse. Toward establishing the function of GARP, we report its three-dimensional structure solved by iodide phasing to a resolution of 1.65 A. An extended helical bundle structure displays an unexpected and significant degree of homology to the core structure of VSG, the only other major surface molecule of trypanosomes to be structurally characterized. Immunofluorescence microscopy and immunoaffinity-tandem mass spectrometry were used in conjunction with monoclonal antibodies to map both non-surface-disposed and surface epitopes. Collectively, these studies enabled us to derive a model describing the orientation and assembly of GARP on the surface of trypanosomes. The data presented here suggest the possible structure-function relationships involved in replacement of the bloodstream form VSG by GARP as trypanosomes differentiate in the tsetse vector after a blood meal. Structural Characterization and Epitope Mapping of the Glutamic Acid/Alanine-rich Protein from Trypanosoma congolense: DEFINING ASSEMBLY ON THE PARASITE CELL SURFACE.,Loveless BC, Mason JW, Sakurai T, Inoue N, Razavi M, Pearson TW, Boulanger MJ J Biol Chem. 2011 Jun 10;286(23):20658-65. Epub 2011 Apr 6. PMID:21471223 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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