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| | <StructureSection load='1b00' size='340' side='right'caption='[[1b00]], [[Resolution|resolution]] 1.88Å' scene=''> | | <StructureSection load='1b00' size='340' side='right'caption='[[1b00]], [[Resolution|resolution]] 1.88Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1b00]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1B00 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1B00 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1b00]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1B00 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1B00 FirstGlance]. <br> |
| - | </td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1b00 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1b00 OCA], [https://pdbe.org/1b00 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1b00 RCSB], [https://www.ebi.ac.uk/pdbsum/1b00 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1b00 ProSAT]</span></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.88Å</td></tr> |
| | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1b00 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1b00 OCA], [https://pdbe.org/1b00 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1b00 RCSB], [https://www.ebi.ac.uk/pdbsum/1b00 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1b00 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[https://www.uniprot.org/uniprot/PHOB_ECOLI PHOB_ECOLI]] This protein is a positive regulator for the phosphate regulon. Transcription of this operon is positively regulated by PhoB and PhoR when phosphate is limited.
| + | [https://www.uniprot.org/uniprot/PHOB_ECOLI PHOB_ECOLI] This protein is a positive regulator for the phosphate regulon. Transcription of this operon is positively regulated by PhoB and PhoR when phosphate is limited. |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Bacillus coli migula 1895]] | + | [[Category: Escherichia coli]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Coll, M]] | + | [[Category: Coll M]] |
| - | [[Category: Gomis-Ruth, F X]] | + | [[Category: Gomis-Ruth FX]] |
| - | [[Category: Gonzalez, A]] | + | [[Category: Gonzalez A]] |
| - | [[Category: Serrano, L]] | + | [[Category: Serrano L]] |
| - | [[Category: Sola, M]] | + | [[Category: Sola M]] |
| - | [[Category: Activation of the pho regulon]]
| + | |
| - | [[Category: Alpha/beta doubly wound fold]]
| + | |
| - | [[Category: Gene regulation]]
| + | |
| - | [[Category: Phosphate regulation]]
| + | |
| - | [[Category: Transcription factor]]
| + | |
| Structural highlights
Function
PHOB_ECOLI This protein is a positive regulator for the phosphate regulon. Transcription of this operon is positively regulated by PhoB and PhoR when phosphate is limited.
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
PhoB is the response regulator of the two-component signal transduction system activated under phosphate starvation conditions. This protein is a transcription factor that activates more than 30 genes of the pho regulon and consists of two domains: a DNA binding domain and a dimerization domain, the latter being homologous to the receiver domain described for two-component response regulators. Activation by phosphorylation induces dimerization of the protein and the consequent binding to the DNA direct repeat pho box, where it promotes the binding of RNA polymerase. In the absence of phosphorylation, the activating dimerization process can be mimicked by deletion of the DNA binding domain. The three-dimensional crystal structure of the receiver domain of PhoB from Escherichia coli has been solved by multiple anomalous diffraction using a gold derivative obtained by co-crystallization, and refined using data to 1.9 A resolution. The crystal structure reveals an alpha/beta doubly wound fold, similar to other known receivers, the most conspicuous difference being the displacement of helix alpha4 towards its N terminus. The active site includes the acidic triad Asp53 (the site of phosphorylation), Asp10 and Glu9. Lys105, from loop beta5alpha5, and Glu88, from helix alpha4, interact with Asp53 via an H-bond and a water bridge, respectively. In the asymmetric unit of the crystal there are two molecules linked by a complementary hydrophobic surface, which involves helix alpha1, loop beta5alpha5 and the N terminus of helix alpha5, and is connected to the active site through the fully conserved residue Lys105 from loop beta5alpha5. The possibility that this surface is the functional surface used for the activating dimerization is discussed.
Three-dimensional crystal structure of the transcription factor PhoB receiver domain.,Sola M, Gomis-Ruth FX, Serrano L, Gonzalez A, Coll M J Mol Biol. 1999 Jan 15;285(2):675-87. PMID:9878437[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Sola M, Gomis-Ruth FX, Serrano L, Gonzalez A, Coll M. Three-dimensional crystal structure of the transcription factor PhoB receiver domain. J Mol Biol. 1999 Jan 15;285(2):675-87. PMID:9878437 doi:10.1006/jmbi.1998.2326
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