7YK5
Rubisco from Phaeodactylum tricornutum bound to PYCO1(452-592)
Summary for 7YK5
| Entry DOI | 10.2210/pdb7yk5/pdb |
| EMDB information | 33887 35158 35159 35166 |
| Descriptor | Ribulose bisphosphate carboxylase large chain, Multifunctional fusion protein, PYCO1 SSU binding motif, ... (5 entities in total) |
| Functional Keywords | rubisco, phase separation, rubisco linker protein, condensation, pyrenoid, phaeodactylum tricornutum, photosynthesis |
| Biological source | Phaeodactylum tricornutum More |
| Total number of polymer chains | 28 |
| Total formula weight | 576565.86 |
| Authors | Oh, Z.G.,Ang, W.S.L.,Bhushan, S.,Mueller-Cajar, O. (deposition date: 2022-07-21, release date: 2023-06-21) |
| Primary citation | Oh, Z.G.,Ang, W.S.L.,Poh, C.W.,Lai, S.K.,Sze, S.K.,Li, H.Y.,Bhushan, S.,Wunder, T.,Mueller-Cajar, O. A linker protein from a red-type pyrenoid phase separates with Rubisco via oligomerizing sticker motifs. Proc.Natl.Acad.Sci.USA, 120:e2304833120-e2304833120, 2023 Cited by PubMed Abstract: The slow kinetics and poor substrate specificity of the key photosynthetic CO-fixing enzyme Rubisco have prompted the repeated evolution of Rubisco-containing biomolecular condensates known as pyrenoids in the majority of eukaryotic microalgae. Diatoms dominate marine photosynthesis, but the interactions underlying their pyrenoids are unknown. Here, we identify and characterize the Rubisco linker protein PYCO1 from . PYCO1 is a tandem repeat protein containing prion-like domains that localizes to the pyrenoid. It undergoes homotypic liquid-liquid phase separation (LLPS) to form condensates that specifically partition diatom Rubisco. Saturation of PYCO1 condensates with Rubisco greatly reduces the mobility of droplet components. Cryo-electron microscopy and mutagenesis data revealed the sticker motifs required for homotypic and heterotypic phase separation. Our data indicate that the PYCO1-Rubisco network is cross-linked by PYCO1 stickers that oligomerize to bind to the small subunits lining the central solvent channel of the Rubisco holoenzyme. A second sticker motif binds to the large subunit. Pyrenoidal Rubisco condensates are highly diverse and tractable models of functional LLPS. PubMed: 37311001DOI: 10.1073/pnas.2304833120 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (2 Å) |
Structure validation
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