1t6r: Difference between revisions

Revision as of 15:42, 28 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1t6r.png

Template:STRUCTURE 1t6r

Solution structure of TM1442, a putative anti sigma factor antagonist in phosphorylated stateSolution structure of TM1442, a putative anti sigma factor antagonist in phosphorylated state

Template:ABSTRACT PUBMED 16826544

About this StructureAbout this Structure

1T6R is a Single protein structure of sequence from Thermotoga maritima. Full experimental information is available from OCA.

ReferenceReference

Solution structures of the putative anti-sigma-factor antagonist TM1442 from Thermotoga maritima in the free and phosphorylated states., Etezady-Esfarjani T, Placzek WJ, Herrmann T, Wuthrich K, Magn Reson Chem. 2006 Jul;44 Spec No:S61-70. PMID:16826544

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Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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-'''Solution structure of TM1442, a putative anti sigma factor antagonist in phosphorylated state'''
+===Solution structure of TM1442, a putative anti sigma factor antagonist in phosphorylated state===
-==Overview==
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-The NMR structures of the unphosphorylated Thermotoga maritima protein TM1442 at pH 4.8 and of the phosphorylated TM1442 (TM1442-P) at pH 7.0 are presented, and a functional interaction of TM1442 with TM0733 is characterized. Although the NMR spectra of TM1442-P at pH 7.0 are of high quality, detailed NMR studies of unphosphorylated TM1442 could be performed only at slightly acidic pH values and high salt concentration. TM1442 is a putative anti-sigma-factor antagonist related to the sigmaF and sigmaB regulation systems in Bacillus subtilis, which is the component in this system that can be phosphorylated. The kinase TM0733, which shows sequence similarity to the GHKL ATPase/kinase superfamily, was identified as the possible anti-sigma-factor of TM1442 using a bioinformatics analysis. Phosphorylation of TM1442 by TM0733 was confirmed by NMR, mass spectroscopy and native gel electrophoresis, and Ser59 was identified as the phosphorylation site using site-directed mutational analysis. The solution structure of TM1442-P at pH 7.0 has the same global fold as free TM1442 at pH 4.8, with an alpha/beta topology consisting of a central four-stranded beta sheet and three alpha helices, but the regular secondary structure elements wrapping the hydrophobic core of the protein undergo subtle conformational changes upon phosphorylation.
+The line below this paragraph, {{ABSTRACT_PUBMED_16826544}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 16826544 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_16826544}}
 ==About this Structure==
-T6R is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Thermotoga_maritima Thermotoga maritima]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1T6R OCA].
+T6R is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Thermotoga_maritima Thermotoga maritima]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1T6R OCA].
 ==Reference==
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 [[Category: Solution structure]]
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