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9LBN

The composite cryo-EM structure of the head-to-tail connector and head-proximal tail components of bacteriophage phiXacJX1

Summary for 9LBN
Entry DOI10.2210/pdb9lbn/pdb
EMDB information62948
Descriptorportal protein gp1, adaptor protein gp5, stopper protein gp6, ... (5 entities in total)
Functional Keywordsxanthomonas phage, head-to-tail connector, tail, virus
Biological sourceXanthomonas phage phiXacJX1
More
Total number of polymer chains8
Total formula weight188885.57
Authors
Guo, M.,Wang, A.,Zheng, Y.,Liu, C.,Shao, Q.,Fang, Q. (deposition date: 2025-01-03, release date: 2025-05-07, Last modification date: 2025-06-18)
Primary citationGuo, 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.
Cryo-EM structures of a Xanthomonas phage: Insights into viral architecture and implications for the model phage HK97.
Structure, 33:1051-1062.e2, 2025
Cited by
PubMed Abstract: Xanthomonas 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 ΦXacJX1 from siphoviruses. These structures include atomic models for the head, head-to-tail connector and head-proximal portion of the tail. ΦXacJX1'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 ΦXacJX1 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.
PubMed: 40273907
DOI: 10.1016/j.str.2025.03.013
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (3.6 Å)
Structure validation

238895

数据于2025-07-16公开中

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