5UKH

Structure of TelC from Streptococcus intermedius B196

Summary for 5UKH

• Entry DOI: 10.2210/pdb5ukh/pdb
• Descriptor: Uncharacterized protein, CALCIUM ION (3 entities in total)
• Functional Keywords: antibacterial effector protein, lipid ii phosphatase, type vii secretion, esx secretion, unknown function
• Biological source: Streptococcus intermedius B196
• Total number of polymer chains: 1
• Total formula weight: 42055.79

Authors

Whitney, J.C.,Ching, M.Q.,Bryant, D.,Mougous, J.D. (deposition date: 2017-01-22, release date: 2017-07-26, Last modification date: 2024-10-23)

Primary citation

Whitney, J.C.,Peterson, S.B.,Kim, J.,Pazos, M.,Verster, A.J.,Radey, M.C.,Kulasekara, H.D.,Ching, M.Q.,Bullen, N.P.,Bryant, D.,Goo, Y.A.,Surette, M.G.,Borenstein, E.,Vollmer, W.,Mougous, J.D.
A broadly distributed toxin family mediates contact-dependent antagonism between gram-positive bacteria.
Elife, 6:-, 2017

PubMed Abstract: The Firmicutes are a phylum of bacteria that dominate numerous polymicrobial habitats of importance to human health and industry. Although these communities are often densely colonized, a broadly distributed contact-dependent mechanism of interbacterial antagonism utilized by Firmicutes has not been elucidated. Here we show that proteins belonging to the LXG polymorphic toxin family present in mediate cell contact- and Esx secretion pathway-dependent growth inhibition of diverse Firmicute species. The structure of one such toxin revealed a previously unobserved protein fold that we demonstrate directs the degradation of a uniquely bacterial molecule required for cell wall biosynthesis, lipid II. Consistent with our functional data linking LXG toxins to interbacterial interactions in , we show that LXG genes are prevalent in the human gut microbiome, a polymicrobial community dominated by Firmicutes. We speculate that interbacterial antagonism mediated by LXG toxins plays a critical role in shaping Firmicute-rich bacterial communities.

PubMed: 28696203
DOI: 10.7554/eLife.26938

Experimental method

X-RAY DIFFRACTION (1.98 Å)