6LUU

apo- Carbonic Anhydrase II pH 7.8 0 atm CO2

6LUU の概要

• エントリーDOI: 10.2210/pdb6luu/pdb
• 分子名称: Carbonic anhydrase 2, GLYCEROL (3 entities in total)
• 機能のキーワード: metalloenzymes; carbonic anhydrase; enzyme mechanism; metal coordination geometry; proton transfer; biological water dynamics, metal binding protein-lyase complex, metal binding protein/lyase
• 由来する生物種: Homo sapiens (Human)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 29381.16

構造登録者

Kim, C.U.,Kim, J.K. (登録日: 2020-02-02, 公開日: 2020-08-19, 最終更新日: 2023-11-29)

主引用文献

Kim, J.K.,Lee, C.,Lim, S.W.,Adhikari, A.,Andring, J.T.,McKenna, R.,Ghim, C.M.,Kim, C.U.
Elucidating the role of metal ions in carbonic anhydrase catalysis.
Nat Commun, 11:4557-4557, 2020

PubMed Abstract: Why metalloenzymes often show dramatic changes in their catalytic activity when subjected to chemically similar but non-native metal substitutions is a long-standing puzzle. Here, we report on the catalytic roles of metal ions in a model metalloenzyme system, human carbonic anhydrase II (CA II). Through a comparative study on the intermediate states of the zinc-bound native CA II and non-native metal-substituted CA IIs, we demonstrate that the characteristic metal ion coordination geometries (tetrahedral for Zn, tetrahedral to octahedral conversion for Co, octahedral for Ni, and trigonal bipyramidal for Cu) directly modulate the catalytic efficacy. In addition, we reveal that the metal ions have a long-range (~10 Å) electrostatic effect on restructuring water network in the active site. Our study provides evidence that the metal ions in metalloenzymes have a crucial impact on the catalytic mechanism beyond their primary chemical properties.

PubMed: 32917908
DOI: 10.1038/s41467-020-18425-5

実験手法

X-RAY DIFFRACTION (1.2 Å)