1B33

STRUCTURE OF LIGHT HARVESTING COMPLEX OF ALLOPHYCOCYANIN ALPHA AND BETA CHAINS/CORE-LINKER COMPLEX AP*LC7.8

Summary for 1B33

• Entry DOI: 10.2210/pdb1b33/pdb
• Descriptor: ALLOPHYCOCYANIN, ALPHA CHAIN, ALLOPHYCOCYANIN, BETA CHAIN, PHYCOBILISOME 7.8 KD LINKER POLYPEPTIDE, ... (6 entities in total)
• Functional Keywords: light-harvesting protein, cyanobacteria, allophycocyanin, linker polypeptides, complex structure, photosynthesis
• Biological source: Mastigocladus laminosus; More
• Cellular location: Cellular thylakoid membrane; Peripheral membrane protein; Cytoplasmic side: P00315 P00318 P20116
• Total number of polymer chains: 14
• Total formula weight: 230139.04

Authors

Reuter, W.,Wiegand, G.,Huber, R.,Than, M.E. (deposition date: 1998-12-15, release date: 1999-02-23, Last modification date: 2025-02-26)

Primary citation

Reuter, W.,Wiegand, G.,Huber, R.,Than, M.E.
Structural analysis at 2.2 A of orthorhombic crystals presents the asymmetry of the allophycocyanin-linker complex, AP.LC7.8, from phycobilisomes of Mastigocladus laminosus.
Proc.Natl.Acad.Sci.USA, 96:1363-1368, 1999

PubMed Abstract: An electrophoretically purified allophycocyanin-linker complex, AP. LC7.8, from phycobilisomes of Mastigocladus laminosus has been crystallized in the orthorhombic space group P212121. Cryocrystallographic x-ray measurements enabled the structural analysis of the complex at a resolution of 2.2 A. The asymmetric unit contains two side-to-side associated "trimeric" (alphabeta)3 allophycocyanin complexes comprising the linker polypeptide in a defined orientation inside the trimer. The linker representing a protein fold related to the prosegment of procarboxypeptidase A is in contact with only two of the three beta-subunits and directly interacts with the corresponding chromophores of these proteins. In addition to a modulation of the chromophores' spectral properties, the linker polypeptide attracts the alphabeta-subcomplexes, thereby bringing the beta-chromophores closer together. These results will enable interpretations of energy-transfer mechanisms within phycobiliproteins.

PubMed: 9990029
DOI: 10.1073/pnas.96.4.1363

Experimental method

X-RAY DIFFRACTION (2.3 Å)