1B8D
CRYSTAL STRUCTURE OF A PHYCOUROBILIN-CONTAINING PHYCOERYTHRIN
Summary for 1B8D
| Entry DOI | 10.2210/pdb1b8d/pdb |
| Descriptor | PROTEIN (RHODOPHYTAN PHYCOERYTHRIN (ALPHA CHAIN)), PROTEIN (RHODOPHYTAN PHYCOERYTHRIN (BETA CHAIN)), PROTEIN (RHODOPHYTAN PHYCOERYTHRIN (GAMMA CHAIN)), ... (6 entities in total) |
| Functional Keywords | light-harvesting complex, red algae, phycobiliprotein, photosynthesis |
| Biological source | Griffithsia monilis More |
| Cellular location | Plastid, chloroplast thylakoid membrane; Peripheral membrane protein; Stromal side: O36005 Plastid, chloroplast thylakoid membrane; Peripheral membrane protein; Stromal side (By similarity): O36004 |
| Total number of polymer chains | 5 |
| Total formula weight | 78947.25 |
| Authors | Ritter, S.,Hiller, R.G.,Wrench, P.M.,Welte, W.,Diederichs, K. (deposition date: 1999-01-29, release date: 1999-02-18, Last modification date: 2023-08-09) |
| Primary citation | Ritter, S.,Hiller, R.G.,Wrench, P.M.,Welte, W.,Diederichs, K. Crystal structure of a phycourobilin-containing phycoerythrin at 1.90-A resolution. J.Struct.Biol., 126:86-97, 1999 Cited by PubMed Abstract: The structure of R-phycoerythrin (R-PE) from the red alga Griffithsia monilis was solved at 1.90-A resolution by molecular replacement, using the atomic coordinates of cyanobacterial phycocyanin from Fremyella diplosiphon as a model. The crystallographic R factor for the final model is 17.5% (Rfree 22.7%) for reflections in the range 100-1.90 A. The model consists of an (alphabeta)2 dimer with an internal noncrystallographic dyad and a fragment of the gamma-polypeptide. The alpha-polypeptide (164 amino acid residues) has two covalently bound phycoerythrobilins at positions alpha82 and alpha139. The beta-polypeptide (177 residues) has two phycoerythrobilins bound to residues beta82 and beta158 and one phycourobilin covalently attached to rings A and D at residues beta50 and beta61, respectively. The electron density of the gamma-polypeptide is mostly averaged out by threefold crystallographic symmetry, but a dipeptide (Gly-Tyr) and one single Tyr could be modeled. These two tyrosine residues of the gamma-polypeptide are in close proximity to the phycoerythrobilins at position beta82 of two symmetry-related beta-polypeptides and are related by the same noncrystallographic dyad as the (alphabeta)2 dimer. Possible energy transfer pathways are discussed briefly. PubMed: 10388620DOI: 10.1006/jsbi.1999.4106 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.9 Å) |
Structure validation
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