Molecular Structure of a Peroxisomal Matrix Protein Transport Factor, Pex14p
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- SU Jian-Rong
- Graduate School of Science, Kyoto University
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- TAKEDA Kazuki
- Graduate School of Science, Kyoto University
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- TAMURA Shigehiko
- Faculty of Science, Kyushu University Graduate School
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- FUJIKI Yukio
- Faculty of Science, Kyushu University Graduate School
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- MIKI Kunio
- Graduate School of Science, Kyoto University
Bibliographic Information
- Other Title
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- ペルオキシソームにおけるタンパク質輸送因子Pex14pの分子構造
- ペルオキシソーム ニ オケル タンパクシツ ユソウ インシ Pex14p ノ ブンシ コウゾウ
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Description
Peroxisome is an organelle in eukaryotic cells, which functions in various metabolisms such as β-oxidation of very long fatty acids. Peroxisomal matrix proteins synthesized in cytosol are imported into the peroxisome by a dynamic system consisting of over a dozen peroxins, Pex1p to Pex26p. Pex14p is a central component of the peroxisomal matrix protein import machinery. Until now, any structural information of Pex14p has not been elucidated at all. We describe here the crystal structure of the conserved domain of mammalian Pex14p at 1.8 Å resolution. A hydrophobic surface is composed of the conserved residues, of which two phenylalanine residues (Phe35 and Phe52) 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. Other structural studies for peroxins are also reviewed in this report.
Journal
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- Nihon Kessho Gakkaishi
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Nihon Kessho Gakkaishi 51 (4), 245-250, 2009
The Crystallographic Society of Japan
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Details 詳細情報について
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- CRID
- 1390282679062444672
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- NII Article ID
- 10025158395
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- NII Book ID
- AN00188364
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- COI
- 1:CAS:528:DC%2BD1MXhsVOksrnN
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- ISSN
- 18845576
- 03694585
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- NDL BIB ID
- 10525717
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- Text Lang
- ja
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- Data Source
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- JaLC
- NDL
- Crossref
- CiNii Articles
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- Abstract License Flag
- Disallowed