2M08

The solution structure of NmPin, the parvuline of Nitrosopumilus maritimus

2M08 の概要

• エントリーDOI: 10.2210/pdb2m08/pdb
• NMR情報: BMRB: 18801
• 分子名称: PpiC-type peptidyl-prolyl cis-trans isomerase (1 entity in total)
• 機能のキーワード: parvulin, archaeal, membrane, thaumarchaeota, sdpar, isomerase
• 由来する生物種: Nitrosopumilus maritimus
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 10197.92

構造登録者

Lederer, C.,Bayer, P. (登録日: 2012-10-22, 公開日: 2014-04-23, 最終更新日: 2024-05-15)

主引用文献

Hoppstock, L.,Trusch, F.,Lederer, C.,van West, P.,Koenneke, M.,Bayer, P.
NmPin from the marine thaumarchaeote Nitrosopumilus maritimus is an active membrane associated prolyl isomerase.
Bmc Biol., 14:53-53, 2016

PubMed Abstract: Peptidyl-prolyl isomerases (PPIases) are present in all forms of life and play a crucial role in protein folding and regulation. They catalyze the cis-trans isomerization of the peptide bond that precedes proline residues in numerous proteins. The parvulins, which is one family of PPIases, have been extensively investigated in several eukaryotes. However, nothing is known about their expression, function and localization in archaea.

PubMed: 27349962
DOI: 10.1186/s12915-016-0274-1

実験手法

SOLUTION NMR