7LGN

Cyanophycin synthetase 1 from T. morbirosei

Summary for 7LGN

• Entry DOI: 10.2210/pdb7lgn/pdb
• Descriptor: Cyanophycin synthase (1 entity in total)
• Functional Keywords: cyanophycin, cpha1, atp-grasp, ligase
• Biological source: Tatumella morbirosei
• Total number of polymer chains: 2
• Total formula weight: 197297.09

Authors

Sharon, I.,Schmeing, T.M. (deposition date: 2021-01-20, release date: 2021-08-18, Last modification date: 2024-05-22)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (3.1 Å)