6wvf

E.coli DsbB C104S with ubiquinone

spinqualitylabelsall models 6wvf, resolution 2.90Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.9Å Ligands: CRO, UQ1 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed Small membrane proteins are difficult targets for structural characterization. Here, we stabilize their folding by restraining their amino and carboxyl termini with associable protein entities, exemplified by the two halves of a superfolder GFP. The termini-restrained proteins are functional and show improved stability during overexpression and purification. The reassembled GFP provides a versatile scaffold for membrane protein crystallization, enables diffraction to atomic resolution, and facilitates crystal identification, phase determination, and density modification. This strategy gives rise to 14 new structures of five vertebrate proteins from distinct functional families, bringing a substantial expansion to the structural database of small membrane proteins. Moreover, a high-resolution structure of bacterial DsbB reveals that this thiol oxidoreductase is activated through a catalytic triad, similar to cysteine proteases. Overall, termini restraining proves exceptionally effective for stabilization and structure determination of small membrane proteins. Termini restraining of small membrane proteins enables structure determination at near-atomic resolution.,Liu S, Li S, Yang Y, Li W Sci Adv. 2020 Dec 18;6(51). pii: 6/51/eabe3717. doi: 10.1126/sciadv.abe3717., Print 2020 Dec. PMID:33355146 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Green Fluorescent Protein 3D structures

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