6EKI

Structure of a hyperthermostable carbonic anhydrase identified from an active hydrothermal vent chimney

6EKI の概要

• エントリーDOI: 10.2210/pdb6eki/pdb
• 分子名称: Carbonic anhydrase, ZINC ION (3 entities in total)
• 機能のキーワード: carbonic anhydrase, thermostability, metagenomics, lyase
• 由来する生物種: Persephonella marina
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 154685.27

構造登録者

Fredslund, F.,Poulsen, J.-C.N.,Lo Leggio, L. (登録日: 2017-09-26, 公開日: 2018-04-11, 最終更新日: 2024-11-20)

主引用文献

Fredslund, F.,Borchert, M.S.,Poulsen, J.N.,Mortensen, S.B.,Perner, M.,Streit, W.R.,Lo Leggio, L.
Structure of a hyperthermostable carbonic anhydrase identified from an active hydrothermal vent chimney.
Enzyme Microb. Technol., 114:48-54, 2018

PubMed Abstract: Carbonic anhydrases (CAs) are extremely fast enzymes, which have attracted much interest in the past due to their medical relevance and their biotechnological potential. An α-type CA gene was isolated from DNA derived from an active hydrothermal vent chimney, in an effort to identify novel CAs with suitable properties for CO capture. The gene product was recombinantly produced and characterized, revealing remarkable thermostability, also in the presence of high ionic strength alkaline conditions, which are used in some CO capture applications. The T was above 90 °C under all tested conditions. The enzyme was crystallized and the structure determined by molecular replacement, revealing a typical bacterial α-type CA non-covalent dimer, but not the disulphide mediated tetramer observed for the hyperthermophilic homologue used for molecular replacement, from Thermovibrio ammonificans. Structural comparison suggests that an increased secondary structure content, increased content of charges on the surface and ionic interactions compared to mesophilic enzymes, may be main structural sources of thermostability, as previously suggested for the homologue from Sulfurihydrogenibium yellowstonense.

PubMed: 29685353
DOI: 10.1016/j.enzmictec.2018.03.009

実験手法

X-RAY DIFFRACTION (2.555 Å)