Structural analysis at 2.2 Å of orthorhombic crystals presents the asymmetry of the allophycocyanin–linker complex, AP⋅L C 7.8 , from phycobilisomes of Mastigocladus laminosus
- 16 February 1999
- journal article
- research article
- Published by Proceedings of the National Academy of Sciences in Proceedings of the National Academy of Sciences of the United States of America
- Vol. 96 (4), 1363-1368
- https://doi.org/10.1073/pnas.96.4.1363
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 Å. The asymmetric unit contains two side-to-side associated “trimeric” (αβ)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 β-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 αβ-subcomplexes, thereby bringing the β-chromophores closer together. These results will enable interpretations of energy-transfer mechanisms within phycobiliproteins.Keywords
This publication has 46 references indexed in Scilit:
- Isolation, crystallization, crystal structure analysis and refinement of allophycocyanin from the cyanobacterium Spirulina platensis at 2.3 Å resolutionJournal of Molecular Biology, 1995
- The CCP4 suite: programs for protein crystallographyActa Crystallographica Section D-Biological Crystallography, 1994
- Isolation, crystallization, crystal structure analysis and refinement of B-phycoerythrin from the red alga Porphyridium sordidum at 2·2 Å resolutionJournal of Molecular Biology, 1992
- Isolation, crystallization, crystal structure analysis and refinement of constitutive C-phycocyanin from the chromatically adapting cyanobacterium Fremyella diplosiphon at 1.66 Å resolutionJournal of Molecular Biology, 1991
- Refined three-dimensional structure of phycoerythrocyanin from the cyanobacterium Mastigocladus laminosus at 2.7 ÅJournal of Molecular Biology, 1990
- Refined three-dimensional structures of two cyanobacterial C-phycocyanins at 2.1 and 2.5 Å resolution: A common principle of phycobilin-protein interactionJournal of Molecular Biology, 1987
- Asymmetrical core structure in phycobilisomes of the cyanobacterium Synechocystis 6701Journal of Molecular Biology, 1986
- Crystal structure analysis and refinement at 2·5 Å of hexameric C-phycocyanin from the cyanobacterium Agmenellum quadruplicatumJournal of Molecular Biology, 1986
- X-ray crystallographic structure of the light-harvesting biliprotein C-phycocyanin from the thermophilic cyanobacterium Mastigocladus laminosus and its resemblance to globin structuresJournal of Molecular Biology, 1985
- Dictionary of protein secondary structure: Pattern recognition of hydrogen‐bonded and geometrical featuresPeptide Science, 1983