5HI8

Structure of T-type Phycobiliprotein Lyase CpeT from Prochlorococcus phage P-HM1

5HI8 の概要

• エントリーDOI: 10.2210/pdb5hi8/pdb
• 分子名称: Antenna protein, MAGNESIUM ION, ACETATE ION, ... (4 entities in total)
• 機能のキーワード: beta barrel, lyase
• 由来する生物種: Prochlorococcus phage P-HM1
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 32685.66

構造登録者

Gasper, R.,Schwach, J.,Frankenberg-Dinkel, N.,Hofmann, E. (登録日: 2016-01-11, 公開日: 2017-01-18, 最終更新日: 2024-10-23)

主引用文献

Gasper, R.,Schwach, J.,Hartmann, J.,Holtkamp, A.,Wiethaus, J.,Riedel, N.,Hofmann, E.,Frankenberg-Dinkel, N.
Distinct Features of Cyanophage-encoded T-type Phycobiliprotein Lyase Phi CpeT: THE ROLE OF AUXILIARY METABOLIC GENES.
J. Biol. Chem., 292:3089-3098, 2017

PubMed Abstract: Auxiliary metabolic genes (AMG) are commonly found in the genomes of phages that infect cyanobacteria and increase the fitness of the cyanophage. AMGs are often homologs of host genes, and also typically related to photosynthesis. For example, the Φ gene in the cyanophage P-HM1 encodes a putative phycobiliprotein lyase related to cyanobacterial T-type lyases, which facilitate attachment of linear tetrapyrrole chromophores to Cys-155 of phycobiliprotein β-subunits, suggesting that ΦCpeT may also help assemble light-harvesting phycobiliproteins during infection. To investigate this possibility, we structurally and biochemically characterized recombinant ΦCpeT. The solved crystal structure of ΦCpeT at 1.8-Å resolution revealed that the protein adopts a similar fold as the cyanobacterial T-type lyase CpcT from sp. PCC7120 but overall is more compact and smaller. ΦCpeT specifically binds phycoerythrobilin (PEB) leading to a tight complex that can also be formed in when it is co-expressed with genes encoding PEB biosynthesis ( and ). The formed ΦCpeT·PEB complex was very stable as the chromophore was not lost during chromatography and displayed a strong red fluorescence with a fluorescence quantum yield of Φ = 0.3. This complex was not directly able to transfer PEB to the host phycobiliprotein β-subunit. However, it could assist the host lyase CpeS in its function by providing a pool of readily available PEB, a feature that might be important for fast phycobiliprotein assembly during phage infection.

PubMed: 28073912
DOI: 10.1074/jbc.M116.769703

実験手法

X-RAY DIFFRACTION (1.8 Å)