1DMX

MURINE MITOCHONDRIAL CARBONIC ANYHDRASE V AT 2.45 ANGSTROMS RESOLUTION

1DMX の概要

• エントリーDOI: 10.2210/pdb1dmx/pdb
• 分子名称: MURINE CARBONIC ANHYDRASE V, ZINC ION (3 entities in total)
• 機能のキーワード: proton transfer, lyase (oxo-acid)
• 由来する生物種: Mus musculus (house mouse)
• 細胞内の位置: Mitochondrion: P23589
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 56682.53

構造登録者

Boriack-Sjodin, P.A.,Christianson, D.W. (登録日: 1995-10-04, 公開日: 1996-04-03, 最終更新日: 2024-02-07)

主引用文献

Boriack-Sjodin, P.A.,Heck, R.W.,Laipis, P.J.,Silverman, D.N.,Christianson, D.W.
Structure determination of murine mitochondrial carbonic anhydrase V at 2.45-A resolution: implications for catalytic proton transfer and inhibitor design.
Proc.Natl.Acad.Sci.USA, 92:10949-10953, 1995

PubMed Abstract: The three-dimensional structure of murine mitochondrial carbonic anhydrase V has been determined and refined at 2.45-A resolution (crystallographic R factor = 0.187). Significant structural differences unique to the active site of carbonic anhydrase V are responsible for differences in the mechanism of catalytic proton transfer as compared with other carbonic anhydrase isozymes. In the prototypical isozyme, carbonic anhydrase II, catalytic proton transfer occurs via the shuttle group His-64; carbonic anhydrase V has Tyr-64, which is not an efficient proton shuttle due in part to the bulky adjacent side chain of Phe-65. Based on analysis of the structure of carbonic anhydrase V, we speculate that Tyr-131 may participate in proton transfer due to its proximity to zinc-bound solvent, its solvent accessibility, and its electrostatic environment in the protein structure. Finally, the design of isozyme-specific inhibitors is discussed in view of the complex between carbonic anhydrase V and acetazolamide, a transition-state analogue. Such inhibitors may be physiologically important in the regulation of blood glucose levels.

PubMed: 7479916
DOI: 10.1073/pnas.92.24.10949

実験手法

X-RAY DIFFRACTION (2.45 Å)