1RRC

T4 POLYNUCLEOTIDE KINASE BOUND TO 5'-GTC-3' SSDNA

1RRC の概要

• エントリーDOI: 10.2210/pdb1rrc/pdb
• 関連するPDBエントリー: 1RC8 1RPZ
• 分子名称: 5'-D(*GP*TP*C)-3', Polynucleotide kinase, CALCIUM ION, ... (6 entities in total)
• 機能のキーワード: kinase, phosphatase, alpha/beta, p-loop, ssdna, transferase-dna complex, transferase/dna
• 由来する生物種: Enterobacteria phage T4
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 36697.71

構造登録者

Eastberg, J.H.,Pelletier, J.,Stoddard, B.L. (登録日: 2003-12-08, 公開日: 2004-02-17, 最終更新日: 2024-10-30)

主引用文献

Eastberg, J.H.,Pelletier, J.,Stoddard, B.L.
Recognition of DNA substrates by T4 bacteriophage polynucleotide kinase.
Nucleic Acids Res., 32:653-660, 2004

PubMed Abstract: T4 phage polynucleotide kinase (PNK) displays 5'-hydroxyl kinase, 3'-phosphatase and 2',3'-cyclic phosphodiesterase activities. The enzyme phosphorylates the 5' hydroxyl termini of a wide variety of nucleic acid substrates, a behavior studied here through the determination of a series of crystal structures with single-stranded (ss)DNA oligonucleotide substrates of various lengths and sequences. In these structures, the 5' ribose hydroxyl is buried in the kinase active site in proper alignment for phosphoryl transfer. Depending on the ssDNA length, the first two or three nucleotide bases are well ordered. Numerous contacts are made both to the phosphoribosyl backbone and to the ordered bases. The position, side chain contacts and internucleotide stacking interactions of the ordered bases are strikingly different for a 5'-GT DNA end than for a 5'-TG end. The base preferences displayed at those positions by PNK are attributable to differences in the enzyme binding interactions and in the DNA conformation for each unique substrate molecule.

PubMed: 14754987
DOI: 10.1093/nar/gkh212

実験手法

X-RAY DIFFRACTION (2.46 Å)