7LGQ

Cyanophycin synthetase 1 from Synechocystis sp. UTEX2470 with ATP and 8x(Asp-Arg)-Asn

7LGQ の概要

• エントリーDOI: 10.2210/pdb7lgq/pdb
• EMDBエントリー: 23328
• 分子名称: Cyanophycin synthase, 8x(Asp-Arg)-Asn, ADENOSINE-5'-TRIPHOSPHATE, ... (4 entities in total)
• 機能のキーワード: cyanophycin, cpha1, atp-grasp, enzyme, ligase
• 由来する生物種: Synechocystis sp. (strain PCC 6714); 詳細
• タンパク質・核酸の鎖数: 12
• 化学式量合計: 405705.63

構造登録者

Sharon, I.,Grogg, M.,Hilvert, D.,Schmeing, T.M. (登録日: 2021-01-20, 公開日: 2021-08-18, 最終更新日: 2024-10-23)

主引用文献

Sharon, I.,Haque, A.S.,Grogg, M.,Lahiri, I.,Seebach, D.,Leschziner, A.E.,Hilvert, D.,Schmeing, T.M.
Structures and function of the amino acid polymerase cyanophycin synthetase.
Nat.Chem.Biol., 17:1101-1110, 2021

PubMed Abstract: Cyanophycin is a natural biopolymer produced by a wide range of bacteria, consisting of a chain of poly-L-Asp residues with L-Arg residues attached to the β-carboxylate sidechains by isopeptide bonds. Cyanophycin is synthesized from ATP, aspartic acid and arginine by a homooligomeric enzyme called cyanophycin synthetase (CphA1). CphA1 has domains that are homologous to glutathione synthetases and muramyl ligases, but no other structural information has been available. Here, we present cryo-electron microscopy and X-ray crystallography structures of cyanophycin synthetases from three different bacteria, including cocomplex structures of CphA1 with ATP and cyanophycin polymer analogs at 2.6 Å resolution. These structures reveal two distinct tetrameric architectures, show the configuration of active sites and polymer-binding regions, indicate dynamic conformational changes and afford insight into catalytic mechanism. Accompanying biochemical interrogation of substrate binding sites, catalytic centers and oligomerization interfaces combine with the structures to provide a holistic understanding of cyanophycin biosynthesis.

PubMed: 34385683
DOI: 10.1038/s41589-021-00854-y

実験手法

ELECTRON MICROSCOPY (2.7 Å)