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Title | Structures and function of the amino acid polymerase cyanophycin synthetase. |
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Journal, issue, pages | Nat Chem Biol, Vol. 17, Issue 10, Page 1101-1110, Year 2021 |
Publish date | Aug 12, 2021 |
![]() | Itai Sharon / Asfarul S Haque / Marcel Grogg / Indrajit Lahiri / Dieter Seebach / Andres E Leschziner / Donald Hilvert / T Martin Schmeing / ![]() ![]() ![]() |
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 ...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. |
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Methods | EM (single particle) / X-ray diffraction |
Resolution | 2.6 - 4.4 Å |
Structure data | EMDB-23311, PDB-7lg5: EMDB-23325, PDB-7lgj: ![]() EMDB-23326: EMDB-23327, PDB-7lgm: EMDB-23328, PDB-7lgq: ![]() PDB-7lgn: |
Chemicals | ![]() ChemComp-ATP: ![]() ChemComp-MG: ![]() ChemComp-ACP: |
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