1XFO

Crystal Structure of an archaeal aminopeptidase

1XFO の概要

• エントリーDOI: 10.2210/pdb1xfo/pdb
• 分子名称: Frv operon protein FrvX, ZINC ION (3 entities in total)
• 機能のキーワード: aminopeptidase, self-compartmentalizing, metalloprotease, dinuclear, hydrolase
• 由来する生物種: Pyrococcus horikoshii
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 158565.26

構造登録者

Russo, S.,Baumann, U. (登録日: 2004-09-15, 公開日: 2004-10-05, 最終更新日: 2023-10-25)

主引用文献

Russo, S.,Baumann, U.
Crystal structure of a dodecameric tetrahedral shaped aminopeptidase
J.Biol.Chem., 279:51275-51281, 2004

PubMed Abstract: Protein turnover is an essential process in living cells. The degradation of cytosolic polypeptides is mainly carried out by the proteasome, resulting in 7-9-amino acid long peptides. Further degradation is usually carried out by energy-independent proteases like the tricorn protease from Thermoplasma acidophilum. Recently, a novel tetrahedral-shaped dodecameric 480-kDa aminopeptidase complex (TET) has been described in Haloarcula marismortui that differs from the known ring- or barrel-shaped self-compartmentalizing proteases. This complex is capable of degrading most peptides down to amino acids. We present here the crystal structure of the tetrahedral aminopeptidase homolog FrvX from Pyrococcus horikoshii. The monomer has a typical clan MH fold, as found for example in Aeromonas proteolytica aminopeptidase, containing a dinuclear zinc active center. The quaternary structure is built by dimers with a length of 100 A that form the edges of the tetrahedron. All 12 active sites are located on the inside of the tetrahedron. Substrate access is granted by pores with a maximal diameter of 10 A, allowing only small peptides and unfolded proteins access to the active site.

PubMed: 15375159
DOI: 10.1074/jbc.M409455200

実験手法

X-RAY DIFFRACTION (1.96 Å)