5EX2

Crystal structure of cyclophilin AquaCyp293 from Hirschia baltica

5EX2 の概要

• エントリーDOI: 10.2210/pdb5ex2/pdb
• 分子名称: Peptidyl-prolyl cis-trans isomerase, MAGNESIUM ION, CALCIUM ION, ... (5 entities in total)
• 機能のキーワード: cyclophilin, ppiase, rotamase, folding helper, periplasmic, isomerase
• 由来する生物種: Hirschia baltica
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 61302.93

構造登録者

Jakob, R.P.,Maier, T. (登録日: 2015-11-23, 公開日: 2016-06-22, 最終更新日: 2024-11-20)

主引用文献

Jakob, R.P.,Schmidpeter, P.A.,Koch, J.R.,Schmid, F.X.,Maier, T.
Structural and Functional Characterization of a Novel Family of Cyclophilins, the AquaCyps.
Plos One, 11:e0157070-e0157070, 2016

PubMed Abstract: Cyclophilins are ubiquitous cis-trans-prolyl isomerases (PPIases) found in all kingdoms of life. Here, we identify a novel family of cyclophilins, termed AquaCyps, which specifically occurs in marine Alphaproteobacteria, but not in related terrestric species. In addition to a canonical PPIase domain, AquaCyps contain large extensions and insertions. The crystal structures of two representatives from Hirschia baltica, AquaCyp293 and AquaCyp300, reveal the formation of a compact domain, the NIC domain, by the N- and C-terminal extensions together with a central insertion. The NIC domain adopts a novel mixed alpha-helical, beta-sheet fold that is linked to the cyclophilin domain via a conserved disulfide bond. In its overall fold, AquaCyp293 resembles AquaCyp300, but the two proteins utilize distinct sets of active site residues, consistent with differences in their PPIase catalytic properties. While AquaCyp293 is a highly active general PPIase, AquaCyp300 is specific for hydrophobic substrate peptides and exhibits lower overall activity.

PubMed: 27276069
DOI: 10.1371/journal.pone.0157070

実験手法

X-RAY DIFFRACTION (1.294 Å)