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1t8b

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[[Image:1t8b.jpg|left|200px]]
 
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==Crystal structure of refolded PHOU-like protein (gi 2983430) from Aquifex aeolicus==
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The line below this paragraph, containing "STRUCTURE_1t8b", creates the "Structure Box" on the page.
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<StructureSection load='1t8b' size='340' side='right'caption='[[1t8b]], [[Resolution|resolution]] 3.23&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[1t8b]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Aquifex_aeolicus Aquifex aeolicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1T8B OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1T8B FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.23&#8491;</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1t8b FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1t8b OCA], [https://pdbe.org/1t8b PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1t8b RCSB], [https://www.ebi.ac.uk/pdbsum/1t8b PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1t8b ProSAT], [https://www.topsan.org/Proteins/BSGC/1t8b TOPSAN]</span></td></tr>
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{{STRUCTURE_1t8b| PDB=1t8b | SCENE= }}
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</table>
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== Function ==
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'''Crystal structure of refolded PHOU-like protein (gi 2983430) from Aquifex aeolicus'''
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[https://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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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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==Overview==
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/t8/1t8b_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1t8b ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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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.
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.
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==About this Structure==
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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>
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1T8B is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Aquifex_aeolicus Aquifex aeolicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1T8B OCA].
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==Reference==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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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:[http://www.ncbi.nlm.nih.gov/pubmed/15937186 15937186]
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</div>
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<div class="pdbe-citations 1t8b" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
[[Category: Aquifex aeolicus]]
[[Category: Aquifex aeolicus]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Adams, P D.]]
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[[Category: Adams PD]]
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[[Category: BSGC, Berkeley Structural Genomics Center.]]
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[[Category: Jancarik J]]
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[[Category: Jancarik, J.]]
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[[Category: Kim R]]
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[[Category: Kim, R.]]
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[[Category: Kim S-H]]
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[[Category: Kim, S H.]]
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[[Category: Oganesyan N]]
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[[Category: Oganesyan, N.]]
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[[Category: Oganesyan V]]
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[[Category: Oganesyan, V.]]
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[[Category: Alpha-helical protein consisting of two 3-helix bundle]]
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[[Category: Berkeley structural genomics center]]
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[[Category: Bsgc structure funded by nih]]
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[[Category: Protein structure initiative]]
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[[Category: Psi]]
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[[Category: Structural genomic]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 09:39:42 2008''
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Current revision

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

PDB ID 1t8b

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