7WAC

Trichodesmium erythraeum cyanophycin synthetase 1 (TeCphA1)

7WAC の概要

• エントリーDOI: 10.2210/pdb7wac/pdb
• EMDBエントリー: 32381
• 分子名称: Cyanophycin synthase (1 entity in total)
• 機能のキーワード: cyanophycin, non-ribosomal peptide synthesis, atp, aspartate, arginine, ligase
• 由来する生物種: Trichodesmium erythraeum IMS101
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 396319.66

構造登録者

Kawasaki, M.,Miyakawa, T.,Yang, J.,Adachi, N.,Fujii, A.,Miyauchi, Y.,Muramatsu, T.,Moriya, T.,Senda, T.,Tanokura, M. (登録日: 2021-12-14, 公開日: 2022-09-07, 最終更新日: 2024-06-26)

主引用文献

Miyakawa, T.,Yang, J.,Kawasaki, M.,Adachi, N.,Fujii, A.,Miyauchi, Y.,Muramatsu, T.,Moriya, T.,Senda, T.,Tanokura, M.
Structural bases for aspartate recognition and polymerization efficiency of cyanobacterial cyanophycin synthetase.
Nat Commun, 13:5097-5097, 2022

PubMed Abstract: Cyanophycin is a natural biopolymer consisting of equimolar amounts of aspartate and arginine as the backbone and branched sidechain, respectively. It is produced by a single enzyme, cyanophycin synthetase (CphA1), and accumulates as a nitrogen reservoir during N fixation by most cyanobacteria. A recent structural study showed that three constituent domains of CphA1 function as two distinct catalytic sites and an oligomerization interface in cyanophycin synthesis. However, it remains unclear how the ATP-dependent addition of aspartate to cyanophycin is initiated at the catalytic site of the glutathione synthetase-like domain. Here, we report the cryogenic electron microscopy structures of CphA1, including a complex with aspartate, cyanophycin primer peptide, and ATP analog. These structures reveal the aspartate binding mode and phosphate-binding loop movement to the active site required for the reaction. Furthermore, structural and mutational data show a potential role of protein dynamics in the catalytic efficiency of the arginine condensation reaction.

PubMed: 36042318
DOI: 10.1038/s41467-022-32834-8

実験手法

ELECTRON MICROSCOPY (2.91 Å)