1uoy

The bubble protein from Penicillium brevicompactum Dierckx exudate.

spinqualitylabelsall models 1uoy, resolution 1.50Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1uoy is a 1 chain structure with sequence from Penicillium brevicompactum. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.5Å Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function BUBL_PENBR May act as a toxin. May recognize a molecule or part of a molecule with a negatively charged surface potential. Publication Abstract from PubMed A small cysteine-rich protein, the function of which remains elusive, was discovered in the exudate of a Penicillium species. Crystal diffraction experiments conducted using in-house Cu Kalpha radiation and an R-AXIS IV++ imaging-plate detector yielded high-quality data to 1.4 A, with a distinguishable anomalous signal from sulfur (DeltaF/F = 0.031). This was used to phase the data and solve the structure using a single data set; the 64-residue amino-acid sequence was unambiguously determined from the electron density. It revealed a globular all-beta protein with a hitherto unknown fold, having a surface electrostatic charge distribution that is similar to that of another small secreted fungal protein, the Williopsis mrakii killer toxin. Aligning the charge distribution superimposed the potential recognition sites of the two proteins, suggesting a similar negatively charged target. Solving the structure of the bubble protein using the anomalous sulfur signal from single-crystal in-house Cu Kalpha diffraction data only.,Olsen JG, Flensburg C, Olsen O, Bricogne G, Henriksen A Acta Crystallogr D Biol Crystallogr. 2004 Feb;60(Pt 2):250-5. Epub 2004, Jan 23. PMID:14747700 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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