1KHI

CRYSTAL STRUCTURE OF HEX1

1KHI の概要

• エントリーDOI: 10.2210/pdb1khi/pdb
• 分子名称: Hex1 (2 entities in total)
• 機能のキーワード: hex1, neurospora crassa, membrane sealing, peroxisomal target, structural protein
• 由来する生物種: Neurospora crassa
• 細胞内の位置: Peroxisome: P87252
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 19150.66

構造登録者

Yuan, P.,Swaminathan, K. (登録日: 2001-11-30, 公開日: 2002-11-30, 最終更新日: 2024-05-29)

主引用文献

Yuan, P.,Jedd, G.,Kumaran, D.,Swaminathan, S.,Shio, H.,Hewitt, D.,Chua, N.-H.,Swaminathan, K.
A HEX-1 crystal lattice required for Woronin body function in Neurospora crassa
NAT.STRUCT.BIOL., 10:264-270, 2003

PubMed Abstract: The Woronin body is a dense-core vesicle specific to filamentous ascomycetes (Euascomycetes), where it functions to seal the septal pore in response to cellular damage. The HEX-1 protein self-assembles to form this solid core of the vesicle. Here, we solve the crystal structure of HEX-1 at 1.8 A, which provides the structural basis of its self-assembly. The structure reveals the existence of three intermolecular interfaces that promote the formation of a three-dimensional protein lattice. Consistent with these data, self-assembly is disrupted by mutations in intermolecular contact residues and expression of an assembly-defective HEX-1 mutant results in the production of aberrant Woronin bodies, which possess a soluble noncrystalline core. This mutant also fails to complement a hex-1 deletion in Neurospora crassa, demonstrating that the HEX-1 protein lattice is required for Woronin body function. Although both the sequence and the tertiary structure of HEX-1 are similar to those of eukaryotic initiation factor 5A (eIF-5A), the amino acids required for HEX-1 self-assembly and peroxisomal targeting are absent in eIF-5A. Thus, we propose that a new function has evolved following duplication of an ancestral eIF-5A gene and that this may define an important step in fungal evolution.

PubMed: 12640443
DOI: 10.1038/nsb910

実験手法

X-RAY DIFFRACTION (1.78 Å)