3ff5

Crystal structure of the conserved N-terminal domain of the peroxisomal matrix-protein-import receptor, Pex14p

spinqualitylabelsall models 3ff5, resolution 1.80Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3ff5 is a 2 chain structure with sequence from Rattus norvegicus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.8Å Ligands: DPW Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function PEX14_RAT Peroxisome membrane protein that is an essential component of the peroxisomal import machinery. Functions as a docking factor for the predominantly cytoplasmic PTS1 receptor (PEX5). Plays a key role for peroxisome movement through a direct interaction with tubulin.[UniProtKB:O75381] 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 Pex14p is a central component of the peroxisomal protein import machinery, in which the conserved N-terminal domain mediates dynamic interactions with other peroxins including Pex5p, Pex13p, and Pex19p. Here, we report the crystal structure of the conserved N-terminal domain of Pex14p with a three-helix bundle. A hydrophobic surface is composed of the conserved residues, of which two phenylalanine residues (Phe-35 and Phe-52) protrude to the solvent. Consequently, two putative binding pockets suitable for recognizing the helical WXXXF/Y motif of Pex5p are formed on the surface by the two phenylalanine residues accompanying with positively charged residues. The structural feature agrees well with our earlier findings where F35A/L36A and F52A/L53A mutants were impaired in the interactions with other peroxins such as Pex5p and Pex13p. Pex14p variants each with Phe-to-Ala mutation at positions 35, 52, and 35/52, respectively, were defective in restoring the impaired peroxisomal protein import in pex14 Chinese hamster ovary mutant ZP161 cells. Moreover, in GST pull-down assays His(6)-Pex5pL bound only to GST-Pex14p(25-70), not to any of GST-Pex14p(25-70)F35A, GST-Pex14p(25-70)F52A, and GST-Pex14p(25-70)F35A/F52A. Endogenous Pex5p was recruited to FLAG-Pex14p on peroxisomes in vivo but barely to FLAG-Pex14pF35A, FLAG-Pex14pF52A, and FLAG-Pex14pF35A/F52A. Collectively, Phe-35 and Phe-52 are essential for the Pex14p functions, including the interaction between Pex14p and Pex5p. Crystal structure of the conserved N-terminal domain of the peroxisomal matrix protein import receptor, Pex14p.,Su JR, Takeda K, Tamura S, Fujiki Y, Miki K Proc Natl Acad Sci U S A. 2009 Jan 13;106(2):417-21. Epub 2009 Jan 2. PMID:19122147 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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