7s97 | pdb_00007s97

Structure of the Photoacclimated Light Harvesting Complex PC577 from Hemiselmis pacifica

spinqualitylabelsall models 7s97, resolution 2.35Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 7s97 is a 4 chain structure with sequence from Hemiselmis pacifica. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.35Å Ligands: CYC, DBV Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function A0A067XP79_9CRYP Light-harvesting photosynthetic tetrapyrrole chromophore-protein from the phycobiliprotein complex.[ARBA:ARBA00033724] Publication Abstract from PubMed Cryptophyte algae are well-known for their ability to survive under low light conditions using their auxiliary light harvesting antennas, phycobiliproteins. Mainly acting to absorb light where chlorophyll cannot (500-650 nm), phycobiliproteins also play an instrumental role in helping cryptophyte algae respond to changes in light intensity through the process of photoacclimation. Until recently, photoacclimation in cryptophyte algae was only observed as a change in the cellular concentration of phycobiliproteins; however, an additional photoacclimation response was recently discovered that causes shifts in the phycobiliprotein absorbance peaks following growth under red, blue, or green light. Here, we reproduce this newly identified photoacclimation response in two species of cryptophyte algae and elucidate the origin of the response on the protein level. We compare isolated native and photoacclimated phycobiliproteins for these two species using spectroscopy and mass spectrometry, and we report the X-ray structures of each phycobiliprotein and the corresponding photoacclimated complex. We find that neither the protein sequences nor the protein structures are modified by photoacclimation. We conclude that cryptophyte algae change one chromophore in the phycobiliprotein beta subunits in response to changes in the spectral quality of light. Ultrafast pump-probe spectroscopy shows that the energy transfer is weakly affected by photoacclimation. Controllable Phycobilin Modification: An Alternative Photoacclimation Response in Cryptophyte Algae.,Spangler LC, Yu M, Jeffrey PD, Scholes GD ACS Cent Sci. 2022 Mar 23;8(3):340-350. doi: 10.1021/acscentsci.1c01209. Epub , 2022 Feb 9. PMID:35350600 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

Proteopedia Page Contributors and Editors (what is this?)

OCA