6R76

Crystal structure of trans-3-Hydroxy-L-proline dehydratase from Thermococcus litoralis - open conformation

6R76 の概要

• エントリーDOI: 10.2210/pdb6r76/pdb
• 分子名称: Proline racemase (3 entities in total)
• 機能のキーワード: hydro-lyase, hydroxyproline dehydratase, lyase
• 由来する生物種: Thermococcus litoralis DSM 5473; 詳細
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 166862.61

構造登録者

Ferraris, D.M.,Miggiano, R.,Rizzi, M. (登録日: 2019-03-28, 公開日: 2019-07-03, 最終更新日: 2024-01-24)

主引用文献

Ferraris, D.M.,Miggiano, R.,Watanabe, S.,Rizzi, M.
Structure of Thermococcus litoralis trans-3-hydroxy-l-proline dehydratase in the free and substrate-complexed form.
Biochem.Biophys.Res.Commun., 516:189-195, 2019

PubMed Abstract: Hydroxyprolines (Hyp) are non-standard amino acids derived from the post-translational modification of proteins by prolyl hydroxylase enzymes. Some plants and bacteria produce Hyp, and the isomers trans-3-Hydroxy-l-proline (T3LHyp) and trans-4-Hydroxy-l-proline (T4LHyp) are major components of mammalian collagen. While T4LHyp is metabolised following distinct degradative pathways in mammals and bacteria, T3LHyp metabolic pathway is conserved in bacteria, plants and mammals, and involves a T3LHyp dehydratase (T3LHypD) in the first degradation step. We report here the crystal structure of T3LHypD from the archaea Thermococcus litoralis in the free and substrate-complexed form. The model shows an "open" and a "closed" conformation depending on the presence (or absence) of the substrate in the catalytic site and allows the mapping of the residues involved in ligand recognition. Moreover, the structure highlights the presence of a water molecule interacting with the hydroxy group of the substrate and potentially involved in catalysis. The structure here reported is the first of its family to be elucidated, and represents a valid model for rationalising the substrate specificity and catalysis of T3LHyp dehydratases.

PubMed: 31208721
DOI: 10.1016/j.bbrc.2019.06.021

実験手法

X-RAY DIFFRACTION (2.4 Å)