6l2w | pdb_00006l2w

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

spinqualitylabelsall models 6l2w, resolution 2.29Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6l2w is a 2 chain structure with sequence from Microcystis phage mic1. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed 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% ~ 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 a, which represents a novel fold in the alpha + beta 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. This article is protected by copyright. All rights reserved. Crystal structure of a novel fold protein Gp72 from the freshwater cyanophage Mic1.,Wang Y, Jin H, Yang F, Jiang YL, Zhao YY, Chen ZP, Li WF, Chen Y, Zhou CZ, Li Q Proteins. 2020 Apr 26. doi: 10.1002/prot.25896. PMID:32337767 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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