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7LGJ

Cyanophycin synthetase 1 from Synechocystis sp. UTEX2470 with ADPCP and 8x(Asp-Arg)-NH2

Summary for 7LGJ
Entry DOI10.2210/pdb7lgj/pdb
EMDB information23325
DescriptorCyanophycin synthase, 8x(Asp-Arg)-NH2, MAGNESIUM ION, ... (4 entities in total)
Functional Keywordscyanophycin, cpha, atp-grasp, enzyme, ligase
Biological sourceSynechocystis sp. (strain PCC 6714)
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Total number of polymer chains8
Total formula weight396113.49
Authors
Sharon, I.,Grogg, M.,Hilvert, D.,Schmeing, T.M. (deposition date: 2021-01-20, release date: 2021-08-18, Last modification date: 2024-11-20)
Primary citationSharon, 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: 34385683
DOI: 10.1038/s41589-021-00854-y
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (2.6 Å)
Structure validation

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