8W7N
Crystal structure of the in-cell Cry1Aa purified from Bacillus thuringiensis
Summary for 8W7N
| Entry DOI | 10.2210/pdb8w7n/pdb |
| Descriptor | Pesticidal crystal protein Cry1Aa, UNKNOWN ATOM OR ION (2 entities in total) |
| Functional Keywords | in cell protein crystal, toxin |
| Biological source | Bacillus thuringiensis |
| Total number of polymer chains | 1 |
| Total formula weight | 129834.50 |
| Authors | Tanaka, J.,Abe, S.,Hayakawa, T.,Kojima, M.,Yamashita, K.,Hirata, K.,Ueno, T. (deposition date: 2023-08-31, release date: 2024-03-06, Last modification date: 2024-11-06) |
| Primary citation | Tanaka, J.,Abe, S.,Hayakawa, T.,Kojima, M.,Yamashita, K.,Hirata, K.,Ueno, T. Crystal structure of the in-cell Cry1Aa purified from Bacillus thuringiensis. Biochem.Biophys.Res.Commun., 685:149144-149144, 2023 Cited by PubMed Abstract: 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. PubMed: 37922785DOI: 10.1016/j.bbrc.2023.149144 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3.6 Å) |
Structure validation
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