2AYI

Wild-type AmpT from Thermus thermophilus

2AYI の概要

• エントリーDOI: 10.2210/pdb2ayi/pdb
• 関連するPDBエントリー: 1ZJC
• 分子名称: Aminopeptidase T, ZINC ION (2 entities in total)
• 機能のキーワード: aminopeptidase, metallopeptidase, hydrolase
• 由来する生物種: Thermus thermophilus
• タンパク質・核酸の鎖数: 5
• 化学式量合計: 226054.15

構造登録者

Odintsov, S.G.,Sabala, I.,Bourenkov, G.,Rybin, V.,Bochtler, M. (登録日: 2005-09-07, 公開日: 2005-11-08, 最終更新日: 2023-08-23)

主引用文献

Odintsov, S.G.,Sabala, I.,Bourenkov, G.,Rybin, V.,Bochtler, M.
Substrate Access to the Active Sites in Aminopeptidase T, a Representative of a New Metallopeptidase Clan.
J.Mol.Biol., 354:403-412, 2005

PubMed Abstract: Aminopeptidase T (AmpT) from Thermus thermophilus is a metalloexopeptidase with no similarity to prototypical metallopeptidases with an HExxH or HxxEH motif. The crystal structure of the Staphylococcus aureus homologue of AmpT, which is known as aminopeptidase S (AmpS), has been reported recently. This structure revealed a dimeric protein with a very unusual, elongated shape and a large internal cavity. The active sites were found on the inner walls of the cavity and were entirely shielded from the environment, which suggested either that the dimer in the crystals was not physiologically relevant, or that an inactive conformation had been crystallized. Here, we show by gel-filtration and analytical ultracentrifugation that AmpT, like AmpS, forms dimers in solution, and we present the structure of AmpT in a crystal form with five protomers in the asymmetric unit. The five protomers take conformations that range from fully closed, as in the AmpS structure, to nearly open, so that the active site is almost directly accessible. The different conformations indicate flexibility between the AmpT N and C-domains, and explain how AmpT can be active, although the unusual AmpS dimerization mode applies to AmpT as well.

PubMed: 16242715
DOI: 10.1016/j.jmb.2005.09.042

実験手法

X-RAY DIFFRACTION (3.7 Å)