1se7: Difference between revisions

Revision as of 16:00, 21 February 2008

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

OverviewOverview

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.

About this StructureAbout this Structure

1SE7 is a Protein complex structure of sequences from Enterobacteria phage p21. Full crystallographic 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

Page seeded by OCA on Thu Feb 21 15:00:39 2008

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OCA

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-[[Image:1se7.jpg|left|200px]]<br /><applet load="1se7" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:1se7.jpg|left|200px]]<br /><applet load="1se7" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="1se7" />
 '''Solution structure of the E. coli bacteriophage P1 encoded HOT protein: a homologue of the theta subunit of E. coli DNA polymerase III'''<br />
 ==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.
+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.
 ==About this Structure==
-SE7 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Enterobacteria_phage_p21 Enterobacteria phage p21]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1SE7 OCA].
+SE7 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Enterobacteria_phage_p21 Enterobacteria phage p21]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1SE7 OCA].
 ==Reference==
@@ Line 13: / Line 13: @@
 [[Category: Enterobacteria phage p21]]
 [[Category: Protein complex]]
-[[Category: Chikova, A.K.]]
+[[Category: Chikova, A K.]]
-[[Category: DeRose, E.F.]]
+[[Category: DeRose, E F.]]
-[[Category: Kirby, T.W.]]
+[[Category: Kirby, T W.]]
-[[Category: London, R.E.]]
+[[Category: London, R E.]]
-[[Category: Mueller, G.A.]]
+[[Category: Mueller, G A.]]
-[[Category: Schaaper, R.M.]]
+[[Category: Schaaper, R M.]]
 [[Category: e. coli bacteriophage p1]]
 [[Category: e. coli dna polymerase iii]]
@@ Line 24: / Line 24: @@
 [[Category: hot]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Sun Nov 25 00:20:40 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:00:39 2008''