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Structure paper

TitleStructures and function of the amino acid polymerase cyanophycin synthetase.
Journal, issue, pagesNat Chem Biol, Vol. 17, Issue 10, Page 1101-1110, Year 2021
Publish dateAug 12, 2021
AuthorsItai Sharon / Asfarul S Haque / Marcel Grogg / Indrajit Lahiri / Dieter Seebach / Andres E Leschziner / Donald Hilvert / T Martin Schmeing /
PubMed AbstractCyanophycin 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 ...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.
External linksNat Chem Biol / PubMed:34385683
MethodsEM (single particle) / X-ray diffraction
Resolution2.6 - 4.4 Å
Structure data

23311

7lg5

EMDB-23311, PDB-7lg5:
Synechocystis sp. UTEX2470 Cyanophycin synthetase 1 with ATP
Method: EM (single particle) / Resolution: 2.63 Å

23325

7lgj

EMDB-23325, PDB-7lgj:
Cyanophycin synthetase 1 from Synechocystis sp. UTEX2470 with ADPCP and 8x(Asp-Arg)-NH2
Method: EM (single particle) / Resolution: 2.6 Å

EMDB-23326:
Cyanophycin synthetase 1 from Synechocystis sp. UTEX2470 with ATP and 16x(Asp-Arg)
Method: EM (single particle) / Resolution: 2.6 Å

23327

7lgm

EMDB-23327, PDB-7lgm:
Cyanophycin synthetase from A. baylyi DSM587 with ATP
Method: EM (single particle) / Resolution: 4.4 Å

23328

7lgq

EMDB-23328, PDB-7lgq:
Cyanophycin synthetase 1 from Synechocystis sp. UTEX2470 with ATP and 8x(Asp-Arg)-Asn
Method: EM (single particle) / Resolution: 2.7 Å

PDB-7lgn:
Cyanophycin synthetase 1 from T. morbirosei
Method: X-RAY DIFFRACTION / Resolution: 3.1 Å

Chemicals

ChemComp-ATP:
ADENOSINE-5'-TRIPHOSPHATE / ATP, energy-carrying molecule*YM / Adenosine triphosphate

ChemComp-MG:
Unknown entry

ChemComp-ACP:
PHOSPHOMETHYLPHOSPHONIC ACID ADENYLATE ESTER / AMP-PCP, energy-carrying molecule analogue*YM

Source
  • Synechocystis sp. PCC 6714 (bacteria)
  • synechocystis sp. (strain pcc 6714) (bacteria)
  • synthetic construct (others)
  • Acinetobacter baylyi ADP1 (bacteria)
  • acinetobacter baylyi (strain atcc 33305 / bd413 / adp1) (bacteria)
  • tatumella morbirosei (bacteria)
KeywordsLIGASE / cyanophycin / CphA1 / ATP grasp / CphA / ATP-grasp / enzyme

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