6KFS

Structure of CCM related protein

6KFS の概要

• エントリーDOI: 10.2210/pdb6kfs/pdb
• 分子名称: LCIB_C_CA domain-containing protein, ZINC ION (3 entities in total)
• 機能のキーワード: carbonic anhydrase, proton shuttle, metal binding protein
• 由来する生物種: Phaeodactylum tricornutum (Diatom)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 28463.39

構造登録者

Jin, S.,Gao, Y.G. (登録日: 2019-07-08, 公開日: 2020-07-15, 最終更新日: 2024-03-27)

主引用文献

Jin, S.,Vullo, D.,Bua, S.,Nocentini, A.,Supuran, C.T.,Gao, Y.G.
Structural and biochemical characterization of novel carbonic anhydrases from Phaeodactylum tricornutum.
Acta Crystallogr D Struct Biol, 76:676-686, 2020

PubMed Abstract: Carbonic anhydrases (CAs) are a well characterized family of metalloenzymes that are highly efficient in facilitating the interconversion between carbon dioxide and bicarbonate. Recently, CA activity has been associated with the LCIB (limiting CO-inducible protein B) protein family, which has been an interesting target in aquatic photosynthetic microorganisms. To gain further insight into the catalytic mechanism of this new group of CAs, the X-ray structure of a highly active LCIB homolog (PtLCIB3) from the diatom Phaeodactylum tricornutum was determined. The CA activities of PtLCIB3, its paralog PtLCIB4 and a variety of their mutants were also measured. It was discovered that PtLCIB3 has a classic β-CA fold and its overall structure is highly similar to that of its homolog PtLCIB4. Subtle structural alterations between PtLCIB3 and PtLCIB4 indicate that an alternative proton-shuttle cavity could perhaps be one reason for their remarkable difference in CA activity. A potential alternative proton-shuttle route in the LCIB protein family is suggested based on these results.

PubMed: 32627740
DOI: 10.1107/S2059798320007202

実験手法

X-RAY DIFFRACTION (1.2 Å)