7LGM
Cyanophycin synthetase from A. baylyi DSM587 with ATP
Summary for 7LGM
| Entry DOI | 10.2210/pdb7lgm/pdb |
| EMDB information | 23327 |
| Descriptor | Cyanophycin synthase, ADENOSINE-5'-TRIPHOSPHATE (2 entities in total) |
| Functional Keywords | cyanophycin, cpha1, atp-grasp, ligase |
| Biological source | Acinetobacter baylyi (strain ATCC 33305 / BD413 / ADP1) |
| Total number of polymer chains | 2 |
| Total formula weight | 204581.69 |
| Authors | Sharon, I.,Haque, A.S.,Lahiri, I.,Leschziner, A.,Schmeing, T.M. (deposition date: 2021-01-20, release date: 2021-08-18, Last modification date: 2024-05-29) |
| 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 Cited by 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: 34385683DOI: 10.1038/s41589-021-00854-y PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (4.4 Å) |
Structure validation
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