3D92

Human carbonic anhydrase II bound with substrate carbon dioxide

3D92 の概要

• エントリーDOI: 10.2210/pdb3d92/pdb
• 分子名称: carbonic anhydrase II, ZINC ION, CARBON DIOXIDE, ... (5 entities in total)
• 機能のキーワード: zinc metalloenzyme, substrate-bound, disease mutation, lyase, metal-binding
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Cytoplasm : P00918
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 29626.68

構造登録者

Domsic, J.F.,Avvaru, B.S.,McKenna, R. (登録日: 2008-05-26, 公開日: 2008-09-02, 最終更新日: 2023-08-30)

主引用文献

Domsic, J.F.,Avvaru, B.S.,Kim, C.U.,Gruner, S.M.,Agbandje-McKenna, M.,Silverman, D.N.,McKenna, R.
Entrapment of carbon dioxide in the active site of carbonic anhydrase II
J.Biol.Chem., 283:30766-30771, 2008

PubMed Abstract: The visualization at near atomic resolution of transient substrates in the active site of enzymes is fundamental to fully understanding their mechanism of action. Here we show the application of using CO(2)-pressurized, cryo-cooled crystals to capture the first step of CO(2) hydration catalyzed by the zinc-metalloenzyme human carbonic anhydrase II, the binding of substrate CO(2), for both the holo and the apo (without zinc) enzyme to 1.1A resolution. Until now, the feasibility of such a study was thought to be technically too challenging because of the low solubility of CO(2) and the fast turnover to bicarbonate by the enzyme (Liang, J. Y., and Lipscomb, W. N. (1990) Proc. Natl. Acad. Sci. U. S. A. 87, 3675-3679). These structures provide insight into the long hypothesized binding of CO(2) in a hydrophobic pocket at the active site and demonstrate that the zinc does not play a critical role in the binding or orientation of CO(2). This method may also have a much broader implication for the study of other enzymes for which CO(2) is a substrate or product and for the capturing of transient substrates and revealing hydrophobic pockets in proteins.

PubMed: 18768466
DOI: 10.1074/jbc.M805353200

実験手法

X-RAY DIFFRACTION (1.1 Å)