1SE7

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

Summary for 1SE7

• Entry DOI: 10.2210/pdb1se7/pdb
• NMR Information: BMRB: 6127
• Descriptor: HOMOLOGUE OF THE THETA SUBUNIT OF DNA POLYMERASE III (1 entity in total)
• Functional Keywords: e. coli bacteriophage p1, homologue of theta, hot, e. coli dna polymerase iii, transferase
• Biological source: Enterobacteria phage P1
• Total number of polymer chains: 1
• Total formula weight: 9709.97

Authors

DeRose, E.F.,Kirby, T.W.,Mueller, G.A.,Chikova, A.K.,Schaaper, R.M.,London, R.E. (deposition date: 2004-02-16, release date: 2004-12-14, Last modification date: 2024-05-22)

Primary citation

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

Experimental method

SOLUTION NMR