4ZWI

Surface Lysine Acetylated Human Carbonic Anhydrase II in Complex with a Sulfamate-Based Inhibitor

4ZWI の概要

• エントリーDOI: 10.2210/pdb4zwi/pdb
• 分子名称: Carbonic anhydrase 2, ZINC ION, DIMETHYL SULFOXIDE, ... (5 entities in total)
• 機能のキーワード: acetylated lysines, sulfamate-based inhibitor, lyase-lyase inhibitor complex, lyase/lyase inhibitor
• 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: 30034.47

構造登録者

Lomelino, C.L.,Mahon, B.P.,McKenna, M. (登録日: 2015-05-19, 公開日: 2015-08-26, 最終更新日: 2024-10-23)

主引用文献

Mahon, B.P.,Lomelino, C.L.,Salguero, A.L.,Driscoll, J.M.,Pinard, M.A.,McKenna, R.
Observed surface lysine acetylation of human carbonic anhydrase II expressed in Escherichia coli.
Protein Sci., 24:1800-1807, 2015

PubMed Abstract: Acetylation of surface lysine residues of proteins has been observed in Escherichia coli (E. coli), an organism that has been extensively utilized for recombinant protein expression. This post-translational modification is shown to be important in various processes such as metabolism, stress-response, transcription, and translation. As such, utilization of E. coli expression systems for protein production may yield non-native acetylation events of surface lysine residues. Here we present the crystal structures of wild-type and a variant of human carbonic anhydrase II (hCA II) that have been expressed in E. coli and exhibit surface lysine acetylation and we speculate on the effect this has on the conformational stability of each enzyme. Both structures were determined to 1.6 Å resolution and show clear electron density for lysine acetylation. The lysine acetylation does not distort the structure and the surface lysine acetylation events most likely do not interfere with the biological interpretation. However, there is a reduction in conformational stability in the hCA II variant compared to wild type (∼ 4°C decrease). This may be due to other lysine acetylation events that have occurred but are not visible in the crystal structure due to intrinsic disorder. Therefore, surface lysine acetylation events may affect overall protein stability and crystallization, and should be considered when using E. coli expression systems.

PubMed: 26266677
DOI: 10.1002/pro.2771

実験手法

X-RAY DIFFRACTION (1.6 Å)