7ta5

Crystal structure of cyanophycin synthetase 2 from Gloeothece citriformis

spinqualitylabelsall models 7ta5, resolution 3.00Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 7ta5 is a 1 chain structure with sequence from Gloeothece citriformis. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 3Å Ligands: BCN, TAR, TRS Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function B7KEP8_GLOC7 Publication Abstract from PubMed Cyanophycin is a biopolymer composed of long chains of beta-Asp-Arg. It is widespread in nature, being synthesized by many clades of bacteria, which use it as a cellular reservoir of nitrogen, carbon, and energy. Two enzymes are known to produce cyanophycin: cyanophycin synthetase 1 (CphA1), which builds cyanophycin from the amino acids Asp and Arg by alternating between two separate reactions for backbone extension and side chain modification, and cyanophycin synthetase 2 (CphA2), which polymerizes beta-Asp-Arg dipeptides. CphA2 is evolutionarily related to CphA1, but questions about CphA2's altered structure and function remain unresolved. Cyanophycin and related molecules have drawn interest as green biopolymers. Because it only has a single active site, CphA2 could be more useful than CphA1 for biotechnological applications seeking to produce modified cyanophycin. In this study, we report biochemical assays on nine cyanobacterial CphA2 enzymes and report the crystal structure of CphA2 from Gloeothece citriformis at 3.0 A resolution. The structure reveals a homodimeric, three-domain architecture. One domain harbors the polymerization active site and the two other domains have structural roles. The structure and biochemical assays explain how CphA2 binds and polymerizes beta-Asp-Arg and highlights differences in in vitro oligomerization and activity between CphA2 enzymes. Using the structure and distinct activity profile as a guide, we introduced a single point mutation that converted Gloeothece citriformis CphA2 from a primer-dependent enzyme into a primer-independent enzyme. Structure and Function of the beta-Asp-Arg Polymerase Cyanophycin Synthetase 2.,Sharon I, Grogg M, Hilvert D, Schmeing TM ACS Chem Biol. 2022 Feb 18. doi: 10.1021/acschembio.1c01007. PMID:35179888 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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