3ZGE

Greater efficiency of photosynthetic carbon fixation due to single amino acid substitution

3ZGE の概要

• エントリーDOI: 10.2210/pdb3zge/pdb
• 関連するPDBエントリー: 3ZGB
• 分子名称: C4 PHOSPHOENOLPYRUVATE CARBOXYLASE, ASPARTIC ACID, SULFATE ION, ... (5 entities in total)
• 機能のキーワード: lyase, c4 photosynthetic pathway, carbon fixation, pep carboxylase
• 由来する生物種: FLAVERIA TRINERVIA
• 細胞内の位置: Cytoplasm (By similarity): P30694
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 227555.62

構造登録者

Paulus, J.K.,Schlieper, D.,Groth, G. (登録日: 2012-12-17, 公開日: 2013-02-27, 最終更新日: 2023-12-20)

主引用文献

Paulus, J.K.,Schlieper, D.,Groth, G.
Greater Efficiency of Photosynthetic Carbon Fixation due to Single Amino Acid Substitution
Nat.Commun., 4:1518-, 2013

PubMed Abstract: The C4-photosynthetic carbon cycle is an elaborated addition to the classical C3-photosynthetic pathway, which improves solar conversion efficiency. The key enzyme in this pathway, phosphoenolpyruvate carboxylase, has evolved from an ancestral non-photosynthetic C3 phosphoenolpyruvate carboxylase. During evolution, C4 phosphoenolpyruvate carboxylase has increased its kinetic efficiency and reduced its sensitivity towards the feedback inhibitors malate and aspartate. An open question is the molecular basis of the shift in inhibitor tolerance. Here we show that a single-point mutation is sufficient to account for the drastic differences between the inhibitor tolerances of C3 and C4 phosphoenolpyruvate carboxylases. We solved high-resolution X-ray crystal structures of a C3 phosphoenolpyruvate carboxylase and a closely related C4 phosphoenolpyruvate carboxylase. The comparison of both structures revealed that Arg884 supports tight inhibitor binding in the C3-type enzyme. In the C4 phosphoenolpyruvate carboxylase isoform, this arginine is replaced by glycine. The substitution reduces inhibitor affinity and enables the enzyme to participate in the C4 photosynthesis pathway.

PubMed: 23443546
DOI: 10.1038/NCOMMS2504

実験手法

X-RAY DIFFRACTION (2.49 Å)