4FKC

Recombinant prolidase from Thermococcus sibiricus

4FKC の概要

• エントリーDOI: 10.2210/pdb4fkc/pdb
• 分子名称: Xaa-Pro aminopeptidase, CADMIUM ION (3 entities in total)
• 機能のキーワード: pita-bread structure, prolidase, hydrolase
• 由来する生物種: Thermococcus sibiricus
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 43947.63

構造登録者

Trofimov, A.A.,Slutskaya, E.S.,Polyakov, K.M.,Dorovatovskii, P.V.,Gumerov, V.M.,Popov, V.O. (登録日: 2012-06-13, 公開日: 2012-11-07, 最終更新日: 2023-09-13)

主引用文献

Trofimov, A.A.,Slutskaya, E.A.,Polyakov, K.M.,Dorovatovskii, P.V.,Gumerov, V.M.,Popov, V.O.
Influence of intermolecular contacts on the structure of recombinant prolidase from Thermococcus sibiricus.
Acta Crystallogr.,Sect.F, 68:1275-1278, 2012

PubMed Abstract: Prolidases are peptidases that are specific for dipeptides with proline as the second residue. The structure of recombinant prolidase from the hyperthermophilic archaeon Thermococcus sibiricus (Tsprol) was determined at 2.6 Å resolution. The homodimer of Tsprol is characterized by a complete lack of interactions between the N- and C-terminal domains of the two subunits and hence can be considered to be the most open structure when compared with previously structurally studied prolidases. This structure exists owing to intermolecular coordination bonds between cadmium ions derived from the crystallization solution and histidine residues of a His tag and aspartate and glutamate residues, which link the dimers to each other. This linking leads to the formation of a crystal with a loose packing of protein molecules and low resistance to mechanical influence and temperature increase.

PubMed: 23143231
DOI: 10.1107/S174430911203761X

実験手法

X-RAY DIFFRACTION (2.6 Å)