Download MendeleyStructural analysis at 2.2 A of orthorhombic crystals presents the asymmetry of the allophycocyanin-linker complex, AP.LC7.8, from phycobilisomes of Mastigocladus laminosus.
Reuter, W., Wiegand, G., Huber, R., Than, M.E.(1999) Proc Natl Acad Sci U S A 96: 1363-1368
- PubMed: 9990029
- DOI: https://doi.org/10.1073/pnas.96.4.1363
- Primary Citation of Related Structures:
1B33 - 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.
Organizational Affiliation:
Max-Planck-Institut für Biochemie, Am Klopferspitz 18A, D-82158 Martinsried, Germany.
