8Z20

Crystal structure analysis of thermotolerant Oscillatoria Phycocyanin

Summary for 8Z20

• Entry DOI: 10.2210/pdb8z20/pdb
• Descriptor: Phycocyanin subunit beta, Phycocyanin subunit alpha, PHYCOCYANOBILIN, ... (5 entities in total)
• Functional Keywords: phycocyanin, oscillatoria, thermotolerant, phycobiliproteins, photosynthesis
• Biological source: Oscillatoria sp. N9DM; More
• Total number of polymer chains: 12
• Total formula weight: 225623.81

Authors

Patel, S.N.,Sonani, R.R.,Gupta, G.D.,Upadhyaya, C.T.,Sonavane, B.P.,Singh, N.K.,Kumar, V.,Madamwar, D. (deposition date: 2024-04-12, release date: 2025-04-16, Last modification date: 2025-06-11)

Primary citation

Patel, S.N.,Sonani, R.R.,Gupta, G.D.,Singh, N.K.,Upadhyaya, C.,Sonavane, B.,Amin, S.,Kumar, V.,Madamwar, D.
Structure and stability of phycocyanin from thermotolerant Oscillatoria.
Febs Lett., 599:1420-1432, 2025

PubMed Abstract: Phycocyanin (PC), a pigment-protein complex with diverse biotechnological applications, plays a key role in light energy transfer for photosynthesis in cyanobacteria. PC (O-PC) from a thermotolerant cyanobacteria Oscillatoria sp. N09DM exhibits remarkable stability compared to its mesophilic counterparts, making it highly valuable for industrial and medical applications. To understand the basis of its stability, the crystal structure of O-PC is solved and analysed. Structural analysis reveals a key molecular interaction, including hydrogen bonds, salt bridges and hydrophobic interactions, along with amino acid substitutions that provide the thermal stability. Additionally, structural results provide insights into chromophore-protein interactions for understanding O-PC's role in the efficient transfer of light energy.

PubMed: 40297916
DOI: 10.1002/1873-3468.70048

Experimental method

X-RAY DIFFRACTION (2.5 Å)