1tid: Difference between revisions

Revision as of 06:36, 29 July 2008

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File:1tid.png

Template:STRUCTURE 1tid

Crystal Structures of the ADP and ATP bound forms of the Bacillus Anti-sigma factor SpoIIAB in complex with the Anti-anti-sigma SpoIIAA: Poised for phosphorylation complex with ATP, crystal form ICrystal Structures of the ADP and ATP bound forms of the Bacillus Anti-sigma factor SpoIIAB in complex with the Anti-anti-sigma SpoIIAA: Poised for phosphorylation complex with ATP, crystal form I

Template:ABSTRACT PUBMED 15236958

About this StructureAbout this Structure

1TID is a Protein complex structure of sequences from Geobacillus stearothermophilus. Full crystallographic information is available from OCA.

ReferenceReference

Crystal structures of the ADP and ATP bound forms of the Bacillus anti-sigma factor SpoIIAB in complex with the anti-anti-sigma SpoIIAA., Masuda S, Murakami KS, Wang S, Anders Olson C, Donigian J, Leon F, Darst SA, Campbell EA, J Mol Biol. 2004 Jul 23;340(5):941-56. PMID:15236958

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OCA

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-[[Image:1tid.gif|left|200px]]
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-'''Crystal Structures of the ADP and ATP bound forms of the Bacillus Anti-sigma factor SpoIIAB in complex with the Anti-anti-sigma SpoIIAA: Poised for phosphorylation complex with ATP, crystal form I'''
+===Crystal Structures of the ADP and ATP bound forms of the Bacillus Anti-sigma factor SpoIIAB in complex with the Anti-anti-sigma SpoIIAA: Poised for phosphorylation complex with ATP, crystal form I===
-==Overview==
+<!--
-Cell type-specific transcription during Bacillus sporulation is established by sigma(F), the activity of which is controlled by a regulatory circuit involving the anti-sigma factor and serine kinase SpoIIAB, and the anti-anti-sigma SpoIIAA. When ATP is present in the nucleotide-binding site of SpoIIAB, SpoIIAA is phosphorylated, followed by dissociation. The nucleotide-binding site of SpoIIAB is left bound to ADP. SpoIIAB(ADP) can bind an unphosphorylated molecule of SpoIIAA as a stable binding partner. Thus, in this circuit, SpoIIAA plays a dual role as a substrate of the SpoIIAB kinase activity, as well as a tight binding inhibitor. Crystal structures of both the pre-phosphorylation complex and the inhibitory complex, SpoIIAB(ATP) and SpoIIAB(ADP) bound to SpoIIAA, respectively, have been determined. The structural differences between the two forms are subtle and confined to interactions with the phosphoryl groups of the nucleotides. The structures reveal details of the SpoIIAA:SpoIIAB interactions and how phosphorylated SpoIIAA dissociates from SpoIIAB(ADP). Finally, the results confirm and expand upon the docking model for SpoIIAA function as an anti-anti-sigma in releasing sigma(F) from SpoIIAB.
+The line below this paragraph, {{ABSTRACT_PUBMED_15236958}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 15236958 is the PubMed ID number.
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+{{ABSTRACT_PUBMED_15236958}}
 ==About this Structure==
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 [[Category: Spoiiab]]
 [[Category: Sporulation]]
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