5xsj

XylFII-LytSN complex

spinqualitylabelsall models 5xsj, resolution 2.20Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5xsj is a 2 chain structure with sequence from Clostridium beijerinckii NCIMB 8052. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.202Å Ligands: XYP Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function A6LW07_CLOB8 Publication Abstract from PubMed d-xylose, the main building block of plant biomass, is a pentose sugar that can be used by bacteria as a carbon source for bio-based fuel and chemical production through fermentation. In bacteria, the first step for d-xylose metabolism is signal perception at the membrane. We previously identified a three-component system in Firmicutes bacteria comprising a membrane-associated sensor protein (XylFII), a transmembrane histidine kinase (LytS) for periplasmic d-xylose sensing, and a cytoplasmic response regulator (YesN) that activates the transcription of the target ABC transporter xylFGH genes to promote the uptake of d-xylose. The molecular mechanism underlying signal perception and integration of these processes remains elusive, however. Here we purified the N-terminal periplasmic domain of LytS (LytSN) in a complex with XylFII and determined the conformational structures of the complex in its d-xylose-free and d-xylose-bound forms. LytSN contains a four-helix bundle, and XylFII contains two Rossmann fold-like globular domains with a xylose-binding cleft between them. In the absence of d-xylose, LytSN and XylFII formed a heterodimer. Specific binding of d-xylose to the cleft of XylFII induced a large conformational change that closed the cleft and brought the globular domains closer together. This conformational change led to the formation of an active XylFII-LytSN heterotetramer. Mutations at the d-xylose binding site and the heterotetramer interface diminished heterotetramer formation and impaired the d-xylose-sensing function of XylFII-LytS. Based on these data, we propose a working model of XylFII-LytS that provides a molecular basis for d-xylose utilization and metabolic modification in bacteria. Molecular mechanism of environmental d-xylose perception by a XylFII-LytS complex in bacteria.,Li J, Wang C, Yang G, Sun Z, Guo H, Shao K, Gu Y, Jiang W, Zhang P Proc Natl Acad Sci U S A. 2017 Aug 1;114(31):8235-8240. doi:, 10.1073/pnas.1620183114. Epub 2017 Jul 17. PMID:28716923 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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