1BYS
CRYSTAL STRUCTURE OF NUC COMPLEXED WITH TUNGSTATE
1BYS の概要
| エントリーDOI | 10.2210/pdb1bys/pdb |
| 関連するPDBエントリー | 1BYR |
| 分子名称 | PROTEIN (ENDONUCLEASE), TUNGSTATE(VI)ION (3 entities in total) |
| 機能のキーワード | endonuclease, phosphodiesterase |
| 由来する生物種 | Salmonella typhimurium |
| タンパク質・核酸の鎖数 | 1 |
| 化学式量合計 | 17423.25 |
| 構造登録者 | |
| 主引用文献 | Stuckey, J.A.,Dixon, J.E. Crystal structure of a phospholipase D family member. Nat.Struct.Biol., 6:278-284, 1999 Cited by PubMed Abstract: The first crystal structure of a phospholipase D (PLD) family member has been determined at 2.0 A resolution. The PLD superfamily is defined by a common sequence motif, HxK(x)4D(x)6GSxN, and includes enzymes involved in signal transduction, lipid biosynthesis, endonucleases and open reading frames in pathogenic viruses and bacteria. The crystal structure suggests that residues from two sequence motifs form a single active site. A histidine residue from one motif acts as a nucleophile in the catalytic mechanism, forming a phosphoenzyme intermediate, whereas a histidine residue from the other motif appears to function as a general acid in the cleavage of the phosphodiester bond. The structure suggests that the conserved lysine residues are involved in phosphate binding. Large-scale genomic sequencing revealed that there are many PLD family members. Our results suggest that all of these proteins may possess a common structure and catalytic mechanism. PubMed: 10074947DOI: 10.1038/6716 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (2 Å) |
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