Fig 1.
Characterization of phycobilisomes of Gracilaria chilensis.
A) Absorption(-) and emission(..) spectra. B) Transmission electron micrograph of purified phycobilisomes.The inserts show amplified images. Schematic drawings of PBS are also shown.
Fig 2.
Spectroscopic characterization and oligomerization state of Allophycocyanin.
A) Absorption (-) and emission (--) spectra of purified Allophycocyanin. B) Molecular sieve chromatogram; the standards and the sample are indicated.
Fig 3.
Sequence comparison between α and αII (ApcA and ApcD), β and β18 (Apcb and ApcF) and α and the PB_domain of the LCM (ApcA and ApcE).
Chromophore binding region are enclosed in green rectangles, and the conserved residues are highlighted in green. The cysteine residues that bind the chromophores are shown in red background. The PB-loop sequence is enclosed in blue lines.
Table 1.
Information on the data collection and refinement for the determination of the three dimensional structure of Allophycocyanin from Gracilaria chilensis.
Fig 4.
Crystallographic structure of Allophycocyanin from Gracilaria chilensis.
A) Ribbon representation of the asymmetric unit, the heterodimer. B) A section of the |2F-Fo| omit electron density map is shown for phycocyanobilin in α subunit. The residues interacting with the chromophore are also shown.
Fig 5.
Binding sites of phycocynobilin.
A) Sticks representation of binding site of phycocyanobilin in α subunit of 5TJF (this paper), αII and the PB domain in APC_3. The chromophores are represented in green. B) Sticks representation of β subunit in 5TJF and β18 in APC_3. The chromophores are also in green.
Fig 6.
Structural models proposed for each trimer of Allophycocyanin.
A) Schematic representation of the different composition trimers. B) Structure of APC, APC_1, APC_2, and APC_3.