4PF1

Crystal structure of aminopeptidase from marine sediment archaeon Thaumarchaeota archaeon

4PF1 の概要

• エントリーDOI: 10.2210/pdb4pf1/pdb
• 分子名称: Peptidase S15/CocE/NonD, TRIETHYLENE GLYCOL, GLYCEROL, ... (4 entities in total)
• 機能のキーワード: serine peptidase, single cell genomics, alpha/beta hydrolase fold, structural genomics, psi-biology, midwest center for structural genomics, mcsg, hydrolase
• 由来する生物種: Thaumarchaeota archaeon SCGC AB-539-E09
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 287087.29

構造登録者

Michalska, K.,Chhor, G.,Fayman, K.,Endres, M.,Jedrzejczak, R.,Babnigg, G.,Steen, A.,Lloyd, K.,Joachimiak, A.,Midwest Center for Structural Genomics (MCSG) (登録日: 2014-04-25, 公開日: 2014-06-11, 最終更新日: 2023-09-27)

主引用文献

Michalska, K.,Steen, A.D.,Chhor, G.,Endres, M.,Webber, A.T.,Bird, J.,Lloyd, K.G.,Joachimiak, A.
New aminopeptidase from "microbial dark matter" archaeon.
FASEB J., 29:4071-4079, 2015

PubMed Abstract: Marine sediments host a large population of diverse, heterotrophic, uncultured microorganisms with unknown physiologies that control carbon flow through organic matter decomposition. Recently, single-cell genomics uncovered new key players in these processes, such as the miscellaneous crenarchaeotal group. These widespread archaea encode putative intra- and extracellular proteases for the degradation of detrital proteins present in sediments. Here, we show that one of these enzymes is a self-compartmentalizing tetrameric aminopeptidase with a preference for cysteine and hydrophobic residues at the N terminus of the hydrolyzed peptide. The ability to perform detailed characterizations of enzymes from native subsurface microorganisms, without requiring that those organisms first be grown in pure culture, holds great promise for understanding key carbon transformations in the environment as well as identifying new enzymes for biomedical and biotechnological applications.

PubMed: 26062601
DOI: 10.1096/fj.15-272906

実験手法

X-RAY DIFFRACTION (2.1 Å)