1BYR
CRYSTAL STRUCTURE OF A PHOSPHOLIPASE D FAMILY MEMBER, NUC FROM SALMONELLA TYPHIMURIUM
Summary for 1BYR
| Entry DOI | 10.2210/pdb1byr/pdb |
| Related | 1BYS |
| Descriptor | PROTEIN (ENDONUCLEASE) (2 entities in total) |
| Functional Keywords | endonuclease, phosphodiesterase |
| Biological source | Salmonella typhimurium |
| Total number of polymer chains | 1 |
| Total formula weight | 17175.42 |
| Authors | Stuckey, J.A.,Dixon, J.E. (deposition date: 1998-10-19, release date: 1999-10-19, Last modification date: 2023-12-27) |
| Primary citation | 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 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2 Å) |
Structure validation
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