6L2W

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

Summary for 6L2W

• Entry DOI: 10.2210/pdb6l2w/pdb
• Descriptor: freshwater cyanophage protein (2 entities in total)
• Functional Keywords: hypothetical proteins, structural protein
• Biological source: Microcystis phage Mic1
• Total number of polymer chains: 2
• Total formula weight: 29272.83

Authors

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. (deposition date: 2019-10-07, release date: 2020-05-13, Last modification date: 2024-03-27)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (2.29 Å)