2WL8

X-ray crystal structure of Pex19p

2WL8 の概要

• エントリーDOI: 10.2210/pdb2wl8/pdb
• 関連するPDBエントリー: 2W85
• 分子名称: PEROXISOMAL BIOGENESIS FACTOR 19 (2 entities in total)
• 機能のキーワード: protein transport, biogenesis disorder, zellweger syndrome, membrane, prenylation
• 由来する生物種: HOMO SAPIENS (HUMAN)
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 57472.75

構造登録者

Schueller, N.,Holton, S.J.,Stanley, W.A.,Song, Y.H.,Konarev, P.,Roessle, M.,Erdmann, R.,Schliebs, W.,Wilmanns, M. (登録日: 2009-06-22, 公開日: 2010-06-23, 最終更新日: 2024-05-08)

主引用文献

Schueller, N.,Holton, S.J.,Fodor, K.,Milewski, M.,Konarev, P.,Stanley, W.A.,Wolf, J.,Erdmann, R.,Schliebs, W.,Song, Y.H.,Wilmanns, M.
The Peroxisomal Receptor Pex19P Forms a Helical Mpts Recognition Domain.
Embo J., 29:2491-, 2010

PubMed Abstract: The protein Pex19p functions as a receptor and chaperone of peroxisomal membrane proteins (PMPs). The crystal structure of the folded C-terminal part of the receptor reveals a globular domain that displays a bundle of three long helices in an antiparallel arrangement. Complementary functional experiments, using a range of truncated Pex19p constructs, show that the structured alpha-helical domain binds PMP-targeting signal (mPTS) sequences with about 10 muM affinity. Removal of a conserved N-terminal helical segment from the mPTS recognition domain impairs the ability for mPTS binding, indicating that it forms part of the mPTS-binding site. Pex19p variants with mutations in the same sequence segment abolish correct cargo import. Our data indicate a divided N-terminal and C-terminal structural arrangement in Pex19p, which is reminiscent of a similar division in the Pex5p receptor, to allow separation of cargo-targeting signal recognition and additional functions.

PubMed: 20531392
DOI: 10.1038/EMBOJ.2010.115

実験手法

X-RAY DIFFRACTION (2.05 Å)