1t72

<table><tr><td colspan='2'>[[1t72]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/"aquifex_aeolicus"_huber_and_stetter_2001 "aquifex aeolicus" huber and stetter 2001]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1T72 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1T72 FirstGlance]. <br>

</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>

<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">PHOU, AQ_906 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=63363 "Aquifex aeolicus" Huber and Stetter 2001])</td></tr>

<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=1t72 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1t72 OCA], [http://pdbe.org/1t72 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1t72 RCSB], [http://www.ebi.ac.uk/pdbsum/1t72 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1t72 ProSAT], [http://www.topsan.org/Proteins/BSGC/1t72 TOPSAN]</span></td></tr>

[[http://www.uniprot.org/uniprot/PHOU_AQUAE PHOU_AQUAE]] Plays a role in the regulation of phosphate uptake. In this role, it may bind, possibly as a chaperone, to PhoR, PhoB or a PhoR-PhoB complex to promote dephosphorylation of phospho-PhoB, or inhibit formation of the PhoR-PhoB transitory complex (Probable).

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== Publication Abstract from PubMed ==

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.

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<ref>PMID:15937186</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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<div class="pdbe-citations 1t72" style="background-color:#fffaf0;"></div>

== References ==

<references/>

[[Category: Aquifex aeolicus huber and stetter 2001]]

[[Category: Adams, P D]]

[[Category: Structural genomic]]

[[Category: Jancarik, J]]

[[Category: Kim, R]]

[[Category: Kim, S H]]

[[Category: Oganesyan, N]]

[[Category: Oganesyan, V]]

[[Category: Transport protein]]