5ukh

Structure of TelC from Streptococcus intermedius B196

spinqualitylabelsall models 5ukh, resolution 1.98Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5ukh is a 1 chain structure with sequence from Streptococcus intermedius B196. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.98Å Ligands: CA, MSE Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function T1ZG69_STRIT Publication Abstract from PubMed 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 Streptococcus intermedius 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 S. intermedius, 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. A broadly distributed toxin family mediates contact-dependent antagonism between gram-positive bacteria.,Whitney JC, Peterson SB, Kim J, Pazos M, Verster AJ, Radey MC, Kulasekara HD, Ching MQ, Bullen NP, Bryant D, Goo YA, Surette MG, Borenstein E, Vollmer W, Mougous JD Elife. 2017 Jul 11;6. pii: e26938. doi: 10.7554/eLife.26938. PMID:28696203 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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