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7FCF

Crystal structure of T6SS Hcp protein

This is a non-PDB format compatible entry.
Summary for 7FCF
Entry DOI10.2210/pdb7fcf/pdb
DescriptorFimbrial protein (2 entities in total)
Functional Keywordshexamer, structural protein
Biological sourceChromobacterium haemolyticum
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Total number of polymer chains6
Total formula weight105701.47
Authors
Jobichen, C.,Sivaraman, J. (deposition date: 2021-07-14, release date: 2022-07-20, Last modification date: 2023-11-29)
Primary citationZwe, Y.H.,Yadav, M.,Ten, M.M.Z.,Srinivasan, M.,Jobichen, C.,Sivaraman, J.,Li, D.
Bacterial antagonism of Chromobacterium haemolyticum and characterization of its putative type VI secretion system.
Res.Microbiol., 173:103918-103918, 2022
Cited by
PubMed Abstract: This study reports the isolation of a new Chromobacterium haemolyticum strain named WI5 from a hydroponic farming facility. WI5 exhibited remarkable bacterial antagonistic properties, eliminating Salmonella, Escherichia coli, Listeria monocytogenes and Staphylococcus aureus (initial inoculum load ∼10 CFU/ml) in dual-species co-culture biofilms. Antagonism was strictly contact-dependent and highly influenced by nutrient availability. Next, we identified a complete suite of putative Type VI secretion system (T6SS) genes in the WI5 genome, annotated the gene locus architecture, and determined the crystal structure of hallmark T6SS tube protein Hcp1, which revealed a hexameric ring structure with an outer and inner diameter of 77 and 45 Å, respectively. Structural comparison with homologs showed differences in the key loops connecting the β-strands in which the conserved residues are located, suggesting a role of these residues in the protein function. The T6SS is well-known to facilitate interbacterial competition, and the putative T6SS characterized herein might be responsible for the remarkable antagonism by C. haemolyticum WI5. Collectively, these findings shed light on the nature of bacterial antagonism and a putative key virulence determinant of C. haemolyticum, which might aid in further understanding its potential ecological role in natural habitats.
PubMed: 34906677
DOI: 10.1016/j.resmic.2021.103918
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (3.3 Å)
Structure validation

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