9KHX
Neck structure of Escherichia phage Mu
Summary for 9KHX
| Entry DOI | 10.2210/pdb9khx/pdb |
| EMDB information | 62358 |
| Descriptor | Gene product J, Portal protein (2 entities in total) |
| Functional Keywords | portal, adaptor, phage, viral protein |
| Biological source | Escherichia phage Mu (Bacteriophage Mu) More |
| Total number of polymer chains | 24 |
| Total formula weight | 872339.76 |
| Authors | Zhou, J.Q.,Liu, H.R. (deposition date: 2024-11-11, release date: 2025-02-12, Last modification date: 2025-04-02) |
| Primary citation | Zhou, J.,Wang, L.,Xiao, H.,Chen, W.,Liu, Z.,Song, J.,Zheng, J.,Liu, H. In situ structures of the contractile nanomachine myophage Mu in both its extended and contracted states. J.Virol., 99:e0205624-e0205624, 2025 Cited by PubMed Abstract: Myophage Mu is a representative of contractile nanomachines with a simple tail baseplate. It has the capacity to infect a range of intestinal bacteria and has extensive applications in genetic engineering research. Nevertheless, a comprehensive understanding of the entire structure and contractile mechanisms of Mu remains elusive. Using cryo-electron microscopy (cryo-EM), we resolved the asymmetric structures of Mu in both its extended and contracted states, the latter of which lacked the tail baseplate, at near-atomic resolutions. We built the atomic models for the extended Mu, encompassing the head, the connector complex, the tail, and the simple baseplate. It is noteworthy that we identified the position and structure of the tail tube initiator protein gp43 (referred to as the DNA circularization protein). The protein gp43 plays a crucial role not only in the baseplate assembly and DNA circularization but also in stabilizing the wedge-hub connection and mediating tail contraction. Except for the baseplate structure, the structural comparison of Mu in its extended and contracted states revealed that only the tail sheath protein gp39 and the C-terminus of the tail terminator protein gp37 undergo notable conformational changes to accommodate the tail contraction, whereas the remaining protein components remained unchanged. Our structures exhibited conserved properties among the majority of myophages, thereby providing valuable insights into the contraction mechanisms across myophages and contractile injection systems (CISs). PubMed: 39992138DOI: 10.1128/jvi.02056-24 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.4 Å) |
Structure validation
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