Abstract
4 Interestingly, however, PerCR does not show the specific targeting when introduced into the cells with a protein transfection reagent. To resolve the structural basis for peroxisomal localization of PerCR, we have determined the crystal structure of PerCR at 1.5 A resolution [1]. The structure revealed that the C-terminal PTS1 of each subunit of PerCR was involved in intersubunit interactions and was buried in the interior of the tetrameric molecule. These data indicate that the monomeric form of PerCR whose C-terminal PTS1 is exposed will be recognized by the PTS1 receptor Pex5p in the cytosol and then, is targeted into the peroxisome and thereby forms tetramer. [1] Tanaka et al., Structure 16, 388-397 (2008).
Highlights
Infectious diseases of the nervous system: pathogenesis and worldwide impact Roberto Bruzzone, Monique Dubois-Dalcq, Georges E Grau, Diane E Griffin and Krister Kristensson Meeting abstracts – A single PDF containing all abstracts in this Supplement is available here.
The overall structure of C-Pasteurella multocida toxin (PMT) displays a Trojan horse structure, composed of three domains arranged in feet, body and head subunits with each linker loops, which were designated C1, C2, and C3 domains from the N- to C-terminus, respectively
We found in the C3 domain the Cys-His-Asp catalytic triad that is organized only when the Cys is released from a disulfide bond
Summary
Infectious diseases of the nervous system: pathogenesis and worldwide impact Roberto Bruzzone, Monique Dubois-Dalcq, Georges E Grau, Diane E Griffin and Krister Kristensson Meeting abstracts – A single PDF containing all abstracts in this Supplement is available here. . Structure and function of C-terminal catalytic region of Pasteurella multocida toxin Kengo Kitadokoro*1, Shigeki Kamitani2, Aya Fukui2, Hiromi Toshima2, Masami Miyake2 and Yasuhiko Horiguchi2
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