8w7n

Crystal structure of the in-cell Cry1Aa purified from Bacillus thuringiensis

spinqualitylabelsall models 8w7n, resolution 3.60Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 8w7n is a 1 chain structure with sequence from Bacillus thuringiensis. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 3.6Å Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function CR1AA_BACTA Promotes colloidosmotic lysis by binding to the midgut epithelial cells of many lepidopteran larvae. Publication Abstract from PubMed In-cell protein crystals which spontaneously crystallize in living cells, have recently been analyzed in investigations of their structures and biological functions. The crystals have been challenging to analyze structurally because of their small size. Therefore, the number of in-cell protein crystals in which the native structure has been determined is limited because most of the structures of in-cell crystals have been determined by recrystallization after dissolution. Some proteins have been reported to form intermolecular disulfide bonds in natural protein crystals that stabilize the crystals. Here, we focus on Cry1Aa, a cysteine-rich protein that crystallizes in Bacillus thuringiensis (Bt) and forms disulfide bonds. Previously, the full-length structure of 135 kDa Cry1Ac, which is the same size as Cry1Aa, was determined by recrystallization of dissolved protein from crystals purified from Bt cells. However, the formation of disulfide bonds has not been investigated because it was necessary to replace cysteine residues to prevent aggregation of the soluble protein. In this work, we succeeded in direct X-ray crystallographic analysis using crystals purified from Bt cells and characterized the cross-linked network of disulfide bonds within Cry1Aa crystals. Crystal structure of the in-cell Cry1Aa purified from Bacillus thuringiensis.,Tanaka J, Abe S, Hayakawa T, Kojima M, Yamashita K, Hirata K, Ueno T Biochem Biophys Res Commun. 2023 Dec 10;685:149144. doi: , 10.1016/j.bbrc.2023.149144. Epub 2023 Oct 24. PMID:37922785 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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