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From Proteopedia
Cryo-EM structure of bacteriophage phiXacJX1 capsid
Structural highlights
Publication Abstract from PubMedXanthomonas bacteria are responsible for disease outbreaks in several hundred plant species, causing significant economic losses. Xanthomonas phages have emerged as a promising biocontrol strategy in managing various important plant diseases caused by Xanthomonas bacteria. However, structural information for Xanthomonas phages has remained limited so far. Here, we present high-resolution cryo-electron microscopy (cryo-EM) structures of the Xanthomonas citri phage PhiXacJX1 from siphoviruses. These structures include atomic models for the head, head-to-tail connector and head-proximal portion of the tail. PhiXacJX1's head and head-to-tail connector components show significant protein sequence and structural homology with those of the model siphophage HK97. However, the in-situ structures of head-to-tail connector of phage HK97 remain unavailable. The presented structures of phage PhiXacJX1 enhance our understanding of Xanthomonas phages and the mature virion of phage HK97. They provide a valuable framework for future structural and functional studies on both Xanthomonas phages and phage HK97. Cryo-EM structures of a Xanthomonas phage: Insights into viral architecture and implications for the model phage HK97.,Guo M, Wang A, Zheng Y, Liu C, Shao Q, Deng Y, Li L, Wang Y, Wang X, Shen Y, Qian J, Zhou X, Fang Q Structure. 2025 Apr 15:S0969-2126(25)00133-9. doi: 10.1016/j.str.2025.03.013. PMID:40273907[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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Categories: Large Structures | Xanthomonas phage phiXacJX1 | Fang Q | Guo M | Liu C | Shao Q | Wang A | Zheng Y