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6H9D

Muramidase domain of SpmX from Asticaccaulis excentricus

Summary for 6H9D
Entry DOI10.2210/pdb6h9d/pdb
DescriptorLysozyme, GLYCEROL, CHLORIDE ION, ... (4 entities in total)
Functional Keywordslysozyme, peptidoglycan hydrolase, cell morphogenesis, stalk synthesis, hydrolase
Biological sourceAsticcacaulis excentricus
Total number of polymer chains3
Total formula weight50223.07
Authors
Randich, A.M.,Morlot, C.M.,Brun, Y.V. (deposition date: 2018-08-03, release date: 2019-05-22, Last modification date: 2024-01-17)
Primary citationRandich, A.M.,Kysela, D.T.,Morlot, C.,Brun, Y.V.
Origin of a Core Bacterial Gene via Co-option and Detoxification of a Phage Lysin.
Curr.Biol., 29:1634-1646.e6, 2019
Cited by
PubMed Abstract: Temperate phages constitute a potentially beneficial genetic reservoir for bacterial innovation despite being selfish entities encoding an infection cycle inherently at odds with bacterial fitness. These phages integrate their genomes into the bacterial host during infection, donating new but deleterious genetic material: the phage genome encodes toxic genes, such as lysins, that kill the bacterium during the phage infection cycle. Remarkably, some bacteria have exploited the destructive properties of phage genes for their own benefit by co-opting them as toxins for functions related to bacterial warfare, virulence, and secretion. However, do toxic phage genes ever become raw material for functional innovation? Here, we report on a toxic phage gene whose product has lost its toxicity and has become a domain of a core cellular factor, SpmX, throughout the bacterial order Caulobacterales. Using a combination of phylogenetics, bioinformatics, structural biology, cell biology, and biochemistry, we have investigated the origin and function of SpmX and determined that its occurrence is the result of the detoxification of a phage peptidoglycan hydrolase gene. We show that the retained, attenuated activity of the phage-derived domain plays an important role in proper cell morphology and developmental regulation in representatives of this large bacterial clade. To our knowledge, this is the first observation of a phage gene domestication event in which a toxic phage gene has been co-opted for core cellular function at the root of a large bacterial clade.
PubMed: 31080080
DOI: 10.1016/j.cub.2019.04.032
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.9 Å)
Structure validation

238895

数据于2025-07-16公开中

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