High-Resolution Crystal Structures of Trimeric and Rod Phycocyanin

David, Liron; Marx, A.; Adir, Noam

doi:10.1016/j.jmb.2010.10.036

Cited by 86 publications

(91 citation statements)

References 64 publications

(96 reference statements)

Supporting

Mentioning

Contrasting

Order By: Relevance

“…The crystal structures of some isolated components of PBSs from different species have been determined. These include PEs [12,13], PCs [8,[14][15][16][17], APCs [10,[17][18][19], and linker proteins [10,20] (Supplementary information, Figure S1). The structural layouts of various PBSs have also been suggested in electron microscopic images [21,22].…”

Section: Introductionmentioning

confidence: 99%

Structural organization of an intact phycobilisome and its association with photosystem II

Chang¹,

et al. 2015

View full text Add to dashboard Cite

Phycobilisomes (PBSs) are light-harvesting antennae that transfer energy to photosynthetic reaction centers in cyanobacteria and red algae. PBSs are supermolecular complexes composed of phycobiliproteins (PBPs) that bear chromophores for energy absorption and linker proteins. Although the structures of some individual components have been determined using crystallography, the three-dimensional structure of an entire PBS complex, which is critical for understanding the energy transfer mechanism, remains unknown. Here, we report the structures of an intact PBS and a PBS in complex with photosystem II (PSII) from Anabaena sp. strain PCC 7120 using single-particle electron microscopy in combination with biochemical and molecular analyses. In the PBS structure, all PBP trimers and the conserved linker protein domains were unambiguously located, and the global distribution of all chromophores was determined. We provide evidence that ApcE and ApcF are critical for the formation of a protrusion at the bottom of PBS, which plays an important role in mediating PBS interaction with PSII. Our results provide insights into the molecular architecture of an intact PBS at different assembly levels and provide the basis for understanding how the light energy absorbed by PBS is transferred to PSII.

show abstract

Section: Introductionmentioning

confidence: 99%

Structural organization of an intact phycobilisome and its association with photosystem II

Chang¹,

et al. 2015

View full text Add to dashboard Cite

show abstract

“…2b for atom numbering). The chirality at C2 has been established as R both in the educt (44) and in the product (45)(46)(47), whereas the chromophore structure in the CpcT-PCB complex seems to be more compatible with an in-plane geometry (Fig. 2b), perhaps due to (partial) enolization with a C1ϭC2 double bond.…”

Section: Resultsmentioning

confidence: 99%

“…The resulting N21-acylimmonium cation is stabilized by the negatively charged carboxylate group of Asp-163 on the sterically hindered ␤-face of the chromophore. The C-S bond is then formed by nucleophilic attack of the thiolate at C3 1 of the chromophore from the less hindered ␣-side, resulting in the 3 1 S configuration that distinguishes the ␤155 chromophore from those attached to other sites (46,47,64). Protonation at C3 from the ␣-face would then result in the correct 3R-configuration, with the C2 and C3 substituents in trans-position.…”

Section: Discussionmentioning

confidence: 99%

Structure and Mechanism of the Phycobiliprotein Lyase CpcT

Zhou

Ding

Zeng

et al. 2014

Journal of Biological Chemistry

View full text Add to dashboard Cite

Background: Phycobiliprotein lyases catalyze covalent attachment of chromophores to cyanobacterial antenna proteins. Results: We present crystal structures of a T-type lyase and its complex with phycocyanobilin. Conclusion: The proposed reaction mechanism accounts for chromophore stabilization and regio-and stereospecificity. Significance: This work sheds light on a crucial step in phycobiliprotein maturation and provides a model for other types of phycobiliprotein lyases.

show abstract

“…Phycobilisomes are proteinaceous complexes composed of a series of rods (6 to 8) connected to a central core [40]. The core and rods are made up of phycobiliprotein molecules aggregated in trimeric or hexameric disks, which are organized in cylindrical macrostructures connected and stabilized by unpigmented linker proteins [113] (Fig. 5).…”

Section: The Phycobilisomes Of Cyanophoramentioning

confidence: 99%

The Glaucophyta: the blue-green plants in a nutshell

2015

View full text Add to dashboard Cite

The Glaucophyta is one of the three major lineages of photosynthetic eukaryotes, together with viridiplants and red algae, united in the presumed monophyletic supergroup Archaeplastida. Glaucophytes constitute a key algal lineage to investigate both the origin of primary plastids and the evolution of algae and plants. Glaucophyte plastids possess exceptional characteristics retained from their cyanobacterial ancestor: phycobilisome antennas, a vestigial peptidoglycan wall, and carboxysome-like bodies. These latter two traits are unique among the Archaeplastida and have been suggested as evidence that the glaucophytes diverged earliest during the diversification of this supergroup. Our knowledge of glaucophytes is limited compared to viridiplants and red algae, and this has restricted our capacity to untangle the early evolution of the Archaeplastida. However, in recent years novel genomic and functional data are increasing our understanding of glaucophyte biology. Diverse comparative studies using information from the nuclear genome of Cyanophora paradoxa and recent transcriptomic data from other glaucophyte species provide support for the common origin of Archaeplastida. Molecular and ultrastructural studies have revealed previously unrecognized diversity in the genera Cyanophora and Glaucocystis. Overall, a series of recent findings are modifying our perspective of glaucophyte diversity and providing fresh approaches to investigate the basic biology of this rare algal group in detail.

show abstract

High-Resolution Crystal Structures of Trimeric and Rod Phycocyanin

Cited by 86 publications

References 64 publications

Structural organization of an intact phycobilisome and its association with photosystem II

Structural organization of an intact phycobilisome and its association with photosystem II

Structure and Mechanism of the Phycobiliprotein Lyase CpcT

The Glaucophyta: the blue-green plants in a nutshell

Contact Info

Product

Resources

About