6x84

Sn-glycerol-3-phosphate binding periplasmic protein UgpB from Escherichia coli - W169S, W172S

spinqualitylabelsall models 6x84, resolution 1.25Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6x84 is a 2 chain structure with sequence from Escherichia coli K-12. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.25Å Ligands: GOL Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function UGPB_ECOLI sn-glycerol-3-phosphate and glycerophosphoryl diester-binding protein interacts with the binding protein-dependent transport system UgpACE. Publication Abstract from PubMed Bile salts are secreted into the gastrointestinal tract to aid in the absorption of lipids. In addition, bile salts show potent antimicrobial activity in part by mediating bacterial protein unfolding and aggregation. Here, using a protein folding sensor, we made the surprising discovery that the Escherichia coli periplasmic glycerol-3-phosphate (G3P)-binding protein UgpB can serve, in the absence of its substrate, as a potent molecular chaperone that exhibits anti-aggregation activity against bile salt-induced protein aggregation. The substrate G3P, which is known to accumulate in the later compartments of the digestive system, triggers a functional switch between UgpB's activity as a molecular chaperone and its activity as a G3P transporter. A UgpB mutant unable to bind G3P is constitutively active as a chaperone, and its crystal structure shows that it contains a deep surface groove absent in the G3P-bound wild-type UgpB. Our work illustrates how evolution may be able to convert threats into signals that first activate and then inactivate a chaperone at the protein level in a manner that bypasses the need for ATP. A metabolite binding protein moonlights as a bile-responsive chaperone.,Lee C, Betschinger P, Wu K, Zyla DS, Glockshuber R, Bardwell JC EMBO J. 2020 Sep 3:e104231. doi: 10.15252/embj.2019104231. PMID:32882062 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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