{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"omics_type":["Unknown"],"volume":["32(7)"],"submitter":["Markus LMD"],"funding":["Eidgenössische Technische Hochschule Zürich","Fonds de recherche du Québec – Nature et technologies","McGill University","Canadian Institutes of Health Research"],"pubmed_abstract":["Cyanophycin is a natural polymer composed of a poly-aspartate backbone with arginine attached to each of the aspartate sidechains. Produced by a wide range of bacteria, which mainly use it as a store of fixed nitrogen, it has many promising industrial applications. Cyanophycin can be synthesized from the amino acids Asp and Arg by the widespread cyanophycin synthetase 1 (CphA1), or from the dipeptide β-Asp-Arg by the cyanobacterial enzyme cyanophycin synthetase 2 (CphA2). CphA2 enzymes display a range of oligomeric states, from dimers to dodecamers. Recently, the crystal structure of a CphA2 dimer was solved but could not be obtained in complex with substrate. Here, we report cryo-EM structures of the hexameric CphA2 from Stanieria sp. at ~2.8 Å resolution, both with and without ATP analog"],"journal":["Protein science : a publication of the Protein Society"],"pagination":["e4685"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC10273328"],"repository":["biostudies-literature"],"pubmed_title":["Structure and function of a hexameric cyanophycin synthetase 2."],"pmcid":["PMC10273328"],"pubmed_authors":["Sharon I","Munro K","Strauss M","Hilvert D","Grogg M","Schmeing TM","Markus LMD"],"additional_accession":[]},"is_claimable":false,"name":"Structure and function of a hexameric cyanophycin synthetase 2.","description":"Cyanophycin is a natural polymer composed of a poly-aspartate backbone with arginine attached to each of the aspartate sidechains. Produced by a wide range of bacteria, which mainly use it as a store of fixed nitrogen, it has many promising industrial applications. Cyanophycin can be synthesized from the amino acids Asp and Arg by the widespread cyanophycin synthetase 1 (CphA1), or from the dipeptide β-Asp-Arg by the cyanobacterial enzyme cyanophycin synthetase 2 (CphA2). CphA2 enzymes display a range of oligomeric states, from dimers to dodecamers. Recently, the crystal structure of a CphA2 dimer was solved but could not be obtained in complex with substrate. Here, we report cryo-EM structures of the hexameric CphA2 from Stanieria sp. at ~2.8 Å resolution, both with and without ATP analog","dates":{"release":"2023-01-01T00:00:00Z","publication":"2023 Jul","modification":"2025-07-10T03:08:12.279Z","creation":"2025-04-06T12:22:59.303Z"},"accession":"S-EPMC10273328","cross_references":{"pubmed":["37222490"],"doi":["10.1002/pro.4685"]}}