5NB3

High resolution C-phycoerythrin from marine cyanobacterium Phormidium sp. A09DM at pH 7.5

Summary for 5NB3

• Entry DOI: 10.2210/pdb5nb3/pdb
• Related: 5aqd 5fvb
• Descriptor: Phycoerythrin Alpha subunit,Phycoerythrin Alpha subunit,Phycoerythrin Alpha subunit, Phycoerythrin Beta subunit,Phycoerythrin Beta subunit, PHYCOERYTHROBILIN, ... (9 entities in total)
• Functional Keywords: photosynthesis, marine cyanobacterium phormidium sp.a09dm, c-phycoerythrin, pigment-protein light harvesting complex
• Biological source: Phormidium rubidum A09DM; More
• Cellular location: Cellular thylakoid membrane ; Peripheral membrane protein ; Cytoplasmic side : A0A0E4G455
• Total number of polymer chains: 24
• Total formula weight: 482688.21

Authors

Sonani, R.R.,Roszak, A.W.,Ortmann de Percin Northumberland, C.,Madamwar, D.,Cogdell, R.J. (deposition date: 2017-03-01, release date: 2017-09-27, Last modification date: 2024-01-17)

Primary citation

Sonani, R.R.,Roszak, A.W.,Ortmann de Percin Northumberland, C.,Madamwar, D.,Cogdell, R.J.
An improved crystal structure of C-phycoerythrin from the marine cyanobacterium Phormidium sp. A09DM.
Photosyn. Res., 135:65-78, 2018

PubMed Abstract: C-Phycoerythrin (PE) from Phormidium sp. A09DM has been crystallized using different conditions and its structure determined to atomic resolution (1.14 Å). In order for the pigment present, phycoerythrobilin (PEB), to function as an efficient light-harvesting molecule it must be held rigidly (Kupka and Scheer in Biochim Biophys Acta 1777:94-103, 2008) and, moreover, the different PEB molecules in PE must be arranged, relative to each other, so as to promote efficient energy transfer between them. This improved structure has allowed us to define in great detail the structure of the PEBs and their binding sites. These precise structural details will facilitate theoretical calculations of each PEB's spectroscopic properties. It was possible, however, to suggest a model for which chromophores contribute to the different regions of absorption spectrum and propose a tentative scheme for energy transfer. We show that some subtle differences in one of these PEB binding sites in two of the 12 subunits are caused by crystal contacts between neighboring hexamers in the crystal lattice. This explains some of the differences seen in previous lower resolution structures determined at two different pH values (Kumar et al. in Photosyn Res 129:17-28, 2016).

PubMed: 28918447
DOI: 10.1007/s11120-017-0443-2

Experimental method

X-RAY DIFFRACTION (1.38 Å)