5B5Z

Crystal structure of PtLCIB4 H88A mutant, a homolog of the limiting CO2-inducible protein LCIB

5B5Z の概要

• エントリーDOI: 10.2210/pdb5b5z/pdb
• 関連するPDBエントリー: 5B5X 5B5Y 5B60 5K5W
• 分子名称: PtLCIB4 H88A mutant, ZINC ION (3 entities in total)
• 機能のキーワード: metalloenzyme, metal binding protein
• 由来する生物種: Phaeodactylum tricornutum
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 60612.43

構造登録者

Jin, S.,Sun, J.,Wunder, T.,Tang, D.,Mueller-Caja, O.M.,Gao, Y. (登録日: 2016-05-24, 公開日: 2016-12-07, 最終更新日: 2023-11-08)

主引用文献

Jin, S.,Sun, J.,Wunder, T.,Tang, D.,Cousins, A.B.,Sze, S.K.,Mueller-Cajar, O.,Gao, Y.G.
Structural insights into the LCIB protein family reveals a new group of beta-carbonic anhydrases
Proc. Natl. Acad. Sci. U.S.A., 113:14716-14721, 2016

PubMed Abstract: Aquatic microalgae have evolved diverse CO-concentrating mechanisms (CCMs) to saturate the carboxylase with its substrate, to compensate for the slow kinetics and competing oxygenation reaction of the key photosynthetic CO-fixing enzyme rubisco. The limiting CO-inducible B protein (LCIB) is known to be essential for CCM function in Chlamydomonas reinhardtii To assign a function to this previously uncharacterized protein family, we purified and characterized a phylogenetically diverse set of LCIB homologs. Three of the six homologs are functional carbonic anhydrases (CAs). We determined the crystal structures of LCIB and limiting CO-inducible C protein (LCIC) from C. reinhardtii and a CA-functional homolog from Phaeodactylum tricornutum, all of which harbor motifs bearing close resemblance to the active site of canonical β-CAs. Our results identify the LCIB family as a previously unidentified group of β-CAs, and provide a biochemical foundation for their function in the microalgal CCMs.

PubMed: 27911826
DOI: 10.1073/pnas.1616294113

実験手法

X-RAY DIFFRACTION (1.6 Å)