Structures and function of the amino acid polymerase cyanophycin synthetase
| Autor: | Asfarul S. Haque, Marcel Grogg, Dieter Seebach, T. Martin Schmeing, Andres E. Leschziner, Donald Hilvert, Itai Sharon, Indrajit Lahiri |
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| Rok vydání: | 2021 |
| Předmět: |
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Molecular chemistry.chemical_classification 0303 health sciences Bacteria Protein Conformation 030306 microbiology Chemistry Cyanophycin Gene Expression Regulation Bacterial Cell Biology Gene Expression Regulation Enzymologic Glutathione synthetase Amino acid 03 medical and health sciences chemistry.chemical_compound Enzyme Bacterial Proteins Structural biology Biosynthesis Biochemistry Aspartic acid Peptide Synthases Binding site Molecular Biology 030304 developmental biology |
| Zdroj: | Nature Chemical Biology. 17:1101-1110 |
| ISSN: | 1552-4469 1552-4450 |
| DOI: | 10.1038/s41589-021-00854-y |
| Popis: | 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 A 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. Structures of three cyanophycin synthetases reveal how the constituent glutathione synthetase and muramyl ligase-like domains cooperate to make cyanophycin, a poly-aspartate chain with arginine residues attached to the sidechains by isopeptide bonds. |
| Databáze: | OpenAIRE |
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