3o74

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<StructureSection load='3o74' size='340' side='right'caption='[[3o74]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
<StructureSection load='3o74' size='340' side='right'caption='[[3o74]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[3o74]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Psepk Psepk]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3O74 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3O74 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[3o74]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudomonas_putida_KT2440 Pseudomonas putida KT2440]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3O74 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3O74 FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr>
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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]] 2&#8491;</td></tr>
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<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>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3o75|3o75]]</div></td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ECK0081 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=160488 PSEPK])</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=3o74 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3o74 OCA], [https://pdbe.org/3o74 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3o74 RCSB], [https://www.ebi.ac.uk/pdbsum/3o74 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3o74 ProSAT]</span></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=3o74 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3o74 OCA], [https://pdbe.org/3o74 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3o74 RCSB], [https://www.ebi.ac.uk/pdbsum/3o74 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3o74 ProSAT]</span></td></tr>
</table>
</table>
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<div style="background-color:#fffaf0;">
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== Function ==
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== Publication Abstract from PubMed ==
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[https://www.uniprot.org/uniprot/Q88PQ6_PSEPK Q88PQ6_PSEPK]
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The catabolite repressor/activator (Cra) protein is a global sensor and regulator of carbon fluxes through the central metabolic pathways of gram-negative bacteria. To examine the nature of the effector (or effectors) that signal such fluxes to the protein of Pseudomonas putida, the Cra factor of this soil microorganism has been purified and characterized and its three-dimensional structure determined. Analytical ultracentrifugation, gel filtration, and mobility shift assays showed that the effector-free Cra is a dimer that binds an operator DNA sequence in the promoter region of the fruBKA cluster. Furthermore, fructose 1-phosphate (F1P) was found to most efficiently dissociate the Cra-DNA complex. Thermodynamic parameters of the F1P-Cra-DNA interaction calculated by isothermal titration calorimetry revealed that the factor associates tightly to the DNA sequence 5'-TTAAACGTTTCA-3' (K(D) = 26.3 +/- 3.1 nM) and that F1P binds the protein with an apparent stoichiometry of 1.06 +/- 0.06 molecules per Cra monomer and a K(D) of 209 +/- 20 nM. Other possible effectors, like fructose 1,6-bisphosphate, did not display a significant affinity for the regulator under the assay conditions. Moreover, the structure of Cra and its co-crystal with F1P at a 2-A resolution revealed that F1P fits optimally the geometry of the effector pocket. Our results thus single out F1P as the preferred metabolic effector of the Cra protein of P. putida.
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Fructose 1-phosphate is the preferred effector of the metabolic regulator Cra of Pseudomonas putida.,Chavarria M, Santiago C, Platero R, Krell T, Casasnovas JM, de Lorenzo V J Biol Chem. 2011 Mar 18;286(11):9351-9. Epub 2011 Jan 14. PMID:21239488<ref>PMID:21239488</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 3o74" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Psepk]]
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[[Category: Pseudomonas putida KT2440]]
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[[Category: Casasnovas, J M]]
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[[Category: Casasnovas JM]]
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[[Category: Chavarria, M]]
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[[Category: Chavarria M]]
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[[Category: Krell, T]]
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[[Category: Krell T]]
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[[Category: Lorenzo, V de]]
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[[Category: Platero R]]
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[[Category: Platero, R]]
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[[Category: Santiago C]]
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[[Category: Santiago, C]]
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[[Category: De Lorenzo V]]
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[[Category: Dna]]
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[[Category: Dual transcriptional regulator]]
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[[Category: Transcription]]
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Revision as of 10:03, 14 February 2024

Crystal structure of Cra transcriptional dual regulator from Pseudomonas putida

PDB ID 3o74

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