6L2W

Crystal structure of a novel fold protein Gp72 from the freshwater cyanophage Mic1

6L2W の概要

• エントリーDOI: 10.2210/pdb6l2w/pdb
• 分子名称: freshwater cyanophage protein (2 entities in total)
• 機能のキーワード: hypothetical proteins, structural protein
• 由来する生物種: Microcystis phage Mic1
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 29272.83

構造登録者

Wang, Y.,Jin, H.,Yang, F.,Jiang, Y.L.,Zhao, Y.Y.,Chen, Z.P.,Li, W.F.,Chen, Y.,Zhou, C.Z.,Li, Q. (登録日: 2019-10-07, 公開日: 2020-05-13, 最終更新日: 2024-03-27)

主引用文献

Wang, Y.,Jin, H.,Yang, F.,Jiang, Y.L.,Zhao, Y.Y.,Chen, Z.P.,Li, W.F.,Chen, Y.,Zhou, C.Z.,Li, Q.
Crystal structure of a novel fold protein Gp72 from the freshwater cyanophage Mic1.
Proteins, 88:1226-1232, 2020

PubMed Abstract: Cyanophages, widespread in aquatic systems, are a class of viruses that specifically infect cyanobacteria. Though they play important roles in modulating the homeostasis of cyanobacterial populations, little is known about the freshwater cyanophages, especially those hypothetical proteins of unknown function. Mic1 is a freshwater siphocyanophage isolated from the Lake Chaohu. It encodes three hypothetical proteins Gp65, Gp66, and Gp72, which share an identity of 61.6% to 83%. However, we find these three homologous proteins differ from each other in oligomeric state. Moreover, we solve the crystal structure of Gp72 at 2.3 Å, which represents a novel fold in the α + β class. Structural analyses combined with redox assays enable us to propose a model of disulfide bond mediated oligomerization for Gp72. Altogether, these findings provide structural and biochemical basis for further investigations on the freshwater cyanophage Mic1.

PubMed: 32337767
DOI: 10.1002/prot.25896

実験手法

X-RAY DIFFRACTION (2.29 Å)