1SE7

Solution structure of the E. coli bacteriophage P1 encoded HOT protein: a homologue of the theta subunit of E. coli DNA polymerase III

1SE7 の概要

• エントリーDOI: 10.2210/pdb1se7/pdb
• NMR情報: BMRB: 6127
• 分子名称: HOMOLOGUE OF THE THETA SUBUNIT OF DNA POLYMERASE III (1 entity in total)
• 機能のキーワード: e. coli bacteriophage p1, homologue of theta, hot, e. coli dna polymerase iii, transferase
• 由来する生物種: Enterobacteria phage P1
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 9709.97

構造登録者

DeRose, E.F.,Kirby, T.W.,Mueller, G.A.,Chikova, A.K.,Schaaper, R.M.,London, R.E. (登録日: 2004-02-16, 公開日: 2004-12-14, 最終更新日: 2024-05-22)

主引用文献

Derose, E.F.,Kirby, T.W.,Mueller, G.A.,Chikova, A.K.,Schaaper, R.M.,London, R.E.
Phage Like It HOT: Solution Structure of the Bacteriophage P1-Encoded HOT Protein, a Homolog of the theta Subunit of E. coli DNA Polymerase III
Structure, 12:2221-2231, 2004

PubMed Abstract: DNA polymerase III, the main replicative polymerase of E. coli, contains a small subunit, theta, that binds to the epsilon proofreading subunit and appears to enhance the enzyme's proofreading function--especially under extreme conditions. It was recently discovered that E. coli bacteriophage P1 encodes a theta homolog, named HOT. The (1)H-(15)N HSQC spectrum of HOT exhibits more uniform intensities and less evidence of conformational exchange than that of theta; this uniformity facilitates a determination of the HOT solution structure by NMR. The structure contains three alpha helices, as reported previously for theta; however, the folding topology of the two proteins is very different. Residual dipolar coupling measurements on labeled theta support the conclusion that it is structurally homologous with HOT. As judged by CD measurements, the melting temperature of HOT was 62 degrees C, compared to 56 degrees C for theta, consistent with other data suggesting greater thermal stability of the HOT protein.

PubMed: 15576035
DOI: 10.1016/j.str.2004.09.019

実験手法

SOLUTION NMR