3UI5

Crystal structure of human Parvulin 14

3UI5 の概要

• エントリーDOI: 10.2210/pdb3ui5/pdb
• 関連するPDBエントリー: 3UI4 3UI6
• 分子名称: Peptidyl-prolyl cis-trans isomerase NIMA-interacting 4, SULFATE ION, (4S,5S)-1,2-DITHIANE-4,5-DIOL, ... (5 entities in total)
• 機能のキーワード: peptidyl-prolyl-isomerase, isomerase
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Isoform 1: Nucleus, nucleolus. Isoform 2: Mitochondrion: Q9Y237
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 11743.51

構造登録者

Mueller, J.W.,Link, N.M.,Matena, A.,Hoppstock, L.,Rueppel, A.,Bayer, P.,Blankenfeldt, W. (登録日: 2011-11-04, 公開日: 2011-12-07, 最終更新日: 2024-02-28)

主引用文献

Mueller, J.W.,Link, N.M.,Matena, A.,Hoppstock, L.,Ruppel, A.,Bayer, P.,Blankenfeldt, W.
Crystallographic proof for an extended hydrogen-bonding network in small prolyl isomerases.
J.Am.Chem.Soc., 133:20096-20099, 2011

PubMed Abstract: Parvulins compose a family of small peptidyl-prolyl isomerases (PPIases) involved in protein folding and protein quality control. A number of amino acids in the catalytic cavity are highly conserved, but their precise role within the catalytic mechanism is unknown. The 0.8 Å crystal structure of the prolyl isomerase domain of parvulin Par14 shows the electron density of hydrogen atoms between the D74, H42, H123, and T118 side chains. This threonine residue has previously not been associated with catalysis, but a corresponding T152A mutant of Pin1 shows a dramatic reduction of catalytic activity without compromising protein stability. The observed catalytic tetrad is strikingly conserved in Pin1- and parvulin-type proteins and hence constitutes a common feature of small peptidyl prolyl isomerases.

PubMed: 22081960
DOI: 10.1021/ja2086195

実験手法

X-RAY DIFFRACTION (1.4 Å)