2c0j

CRYSTAL STRUCTURE OF THE BET3-TRS33 HETERODIMER

spinqualitylabelsall models 2c0j, resolution 2.20Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2c0j is a 2 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: PLM Related: 1sz7 Resources: FirstGlance, OCA, RCSB, PDBsum Function [TPPC3_HUMAN] May play a role in vesicular transport from endoplasmic reticulum to Golgi. [TPC6A_HUMAN] May play a role in vesicular transport during the biogenesis of melanosomes (By similarity). Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed Transport protein particle (TRAPP) comprises a family of two highly related multiprotein complexes, with seven common subunits, that serve to target different classes of transport vesicles to their appropriate compartments. Defining the architecture of the complexes will advance our understanding of the functional differences between these highly related molecular machines. Genetic analyses in yeast suggested a specific interaction between the TRAPP subunits Bet3p and Trs33p. A mammalian bet3-trs33 complex was crystallized, and the structure was solved to 2.2 angstroms resolution. Intriguingly, the overall fold of the bet3 and trs33 monomers was similar, although the proteins had little overall sequence identity. In vitro experiments using yeast TRAPP subunits indicated that Bet3p binding to Trs33p facilitates the interaction between Bet3p and another TRAPP subunit, Bet5p. Mutational analysis suggests that yeast Trs33p facilitates other Bet3p protein-protein interactions. Furthermore, we show that Trs33p can increase the Golgi-localized pool of a mutated Bet3 protein normally found in the cytosol. We propose that one of the roles of Trs33p is to facilitate the incorporation of the Bet3p subunit into assembling TRAPP complexes. Biochemical and crystallographic studies reveal a specific interaction between TRAPP subunits Trs33p and Bet3p.,Kim MS, Yi MJ, Lee KH, Wagner J, Munger C, Kim YG, Whiteway M, Cygler M, Oh BH, Sacher M Traffic. 2005 Dec;6(12):1183-95. PMID:16262728 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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