1se7: Difference between revisions

Revision as of 15:50, 28 July 2008

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Template:STRUCTURE 1se7

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

Template:ABSTRACT PUBMED 15576035

About this StructureAbout this Structure

Full experimental information is available from OCA.

ReferenceReference

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., Derose EF, Kirby TW, Mueller GA, Chikova AK, Schaaper RM, London RE, Structure. 2004 Dec;12(12):2221-31. PMID:15576035

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-'''Solution structure of the E. coli bacteriophage P1 encoded HOT protein: a homologue of the theta subunit of E. coli DNA polymerase III'''
+===Solution structure of the E. coli bacteriophage P1 encoded HOT protein: a homologue of the theta subunit of E. coli DNA polymerase III===
-==Overview==
+<!--
-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.
+The line below this paragraph, {{ABSTRACT_PUBMED_15576035}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 15576035 is the PubMed ID number.
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+{{ABSTRACT_PUBMED_15576035}}
 ==About this Structure==
-Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1SE7 OCA].
+Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1SE7 OCA].
 ==Reference==
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 [[Category: Homologue of theta]]
 [[Category: Hot]]
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