1t8b: Difference between revisions

Revision as of 13:18, 29 July 2008

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File:1t8b.png

Template:STRUCTURE 1t8b

Crystal structure of refolded PHOU-like protein (gi 2983430) from Aquifex aeolicusCrystal structure of refolded PHOU-like protein (gi 2983430) from Aquifex aeolicus

Template:ABSTRACT PUBMED 15937186

About this StructureAbout this Structure

1T8B is a Single protein structure of sequence from Aquifex aeolicus. Full crystallographic information is available from OCA.

ReferenceReference

Crystal structure of the "PhoU-like" phosphate uptake regulator from Aquifex aeolicus., Oganesyan V, Oganesyan N, Adams PD, Jancarik J, Yokota HA, Kim R, Kim SH, J Bacteriol. 2005 Jun;187(12):4238-44. PMID:15937186

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OCA

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-'''Crystal structure of refolded PHOU-like protein (gi 2983430) from Aquifex aeolicus'''
+===Crystal structure of refolded PHOU-like protein (gi 2983430) from Aquifex aeolicus===
-==Overview==
+<!--
-The phoU gene of Aquifex aeolicus encodes a protein called PHOU_AQUAE with sequence similarity to the PhoU protein of Escherichia coli. Despite the fact that there is a large number of family members (more than 300) attributed to almost all known bacteria and despite PHOU_AQUAE's association with the regulation of genes for phosphate metabolism, the nature of its regulatory function is not well understood. Nearly one-half of these PhoU-like proteins, including both PHOU_AQUAE and the one from E. coli, form a subfamily with an apparent dimer structure of two PhoU domains on the basis of their amino acid sequence. The crystal structure of PHOU_AQUAE (a 221-amino-acid protein) reveals two similar coiled-coil PhoU domains, each forming a three-helix bundle. The structures of PHOU_AQUAE proteins from both a soluble fraction and refolded inclusion bodies (at resolutions of 2.8 and 3.2A, respectively) showed no significant differences. The folds of the PhoU domain and Bag domains (for a class of cofactors of the eukaryotic chaperone Hsp70 family) are similar. Accordingly, we propose that gene regulation by PhoU may occur by association of PHOU_AQUAE with the ATPase domain of the histidine kinase PhoR, promoting release of its substrate PhoB. Other proteins that share the PhoU domain fold include the coiled-coil domains of the STAT protein, the ribosome-recycling factor, and structural proteins like spectrin.
+The line below this paragraph, {{ABSTRACT_PUBMED_15937186}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 15937186 is the PubMed ID number.
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+{{ABSTRACT_PUBMED_15937186}}
 ==About this Structure==
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 [[Category: Psi]]
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