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| | <StructureSection load='4d6x' size='340' side='right'caption='[[4d6x]], [[Resolution|resolution]] 2.11Å' scene=''> | | <StructureSection load='4d6x' size='340' side='right'caption='[[4d6x]], [[Resolution|resolution]] 2.11Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4d6x]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacterium_abortus"_schmidt_in_schmidt_and_weis_1901 "bacterium abortus" schmidt in schmidt and weis 1901]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4D6X OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4D6X FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4d6x]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Brucella_abortus Brucella abortus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4D6X OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4D6X FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=IMD:IMIDAZOLE'>IMD</scene></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=IMD:IMIDAZOLE'>IMD</scene></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4d6x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4d6x OCA], [http://pdbe.org/4d6x PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4d6x RCSB], [http://www.ebi.ac.uk/pdbsum/4d6x PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4d6x 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=4d6x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4d6x OCA], [https://pdbe.org/4d6x PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4d6x RCSB], [https://www.ebi.ac.uk/pdbsum/4d6x PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4d6x ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [[https://www.uniprot.org/uniprot/Q2YPW6_BRUA2 Q2YPW6_BRUA2]] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Bacterium abortus schmidt in schmidt and weis 1901]] | + | [[Category: Brucella abortus]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Carrica, M C]] | + | [[Category: Carrica MC]] |
| - | [[Category: Fernandez, I]] | + | [[Category: Fernandez I]] |
| - | [[Category: Goldbaum, F A]] | + | [[Category: Goldbaum FA]] |
| - | [[Category: Klinke, S]] | + | [[Category: Klinke S]] |
| - | [[Category: Otero, L H]] | + | [[Category: Otero LH]] |
| - | [[Category: Brucellosis]]
| + | |
| - | [[Category: Microaerobisis]]
| + | |
| - | [[Category: Rec domain]]
| + | |
| - | [[Category: Response regulator]]
| + | |
| - | [[Category: Signaling protein]]
| + | |
| - | [[Category: Two-component system]]
| + | |
| Structural highlights
Function
[Q2YPW6_BRUA2]
Publication Abstract from PubMed
Brucella abortus is an important pathogenic bacterium that has to overcome oxygen deficiency in order to achieve a successful infection. Previously, we proved that a two-component system formed by the histidine kinase NtrY and the response regulator NtrX is essential to achieve an adaptive response to low oxygen tension conditions. Even though the relevance of this signaling pathway has already been demonstrated in other microorganisms, its molecular activation mechanism has not yet been described in detail. In this article, we report the first crystal structures from different conformations of the NtrX receiver domain from B. abortus, and we propose a sequence of events to explain the structural rearrangements along the activation process. The analysis of the structures obtained in the presence of the phosphoryl group analog beryllofluoride led us to postulate that changes in the interface formed by the alpha4 helix and the beta5 strand are important for the activation, producing a reorientation of the alpha5 helix. Also, a biochemical characterization of the NtrX receiver domain enzymatic activities was performed, describing its autophosphorylation and autodephosphorylation kinetics. Finally, the role of H85, an important residue, was addressed by site-directed mutagenesis. Overall, these results provide significant structural basis for understanding the response regulator activation in this bacterial two-component system.
Snapshots of Conformational Changes Shed Light into the NtrX Receiver Domain Signal Transduction Mechanism.,Fernandez I, Otero LH, Klinke S, Carrica MD, Goldbaum FA J Mol Biol. 2015 Jun 23. pii: S0022-2836(15)00350-2. doi:, 10.1016/j.jmb.2015.06.010. PMID:26113057[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Fernandez I, Otero LH, Klinke S, Carrica MD, Goldbaum FA. Snapshots of Conformational Changes Shed Light into the NtrX Receiver Domain Signal Transduction Mechanism. J Mol Biol. 2015 Jun 23. pii: S0022-2836(15)00350-2. doi:, 10.1016/j.jmb.2015.06.010. PMID:26113057 doi:http://dx.doi.org/10.1016/j.jmb.2015.06.010
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