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| | ==Structure of Citrate-free Periplasmic Domain of Sensor Histidine Kinase CitA== | | ==Structure of Citrate-free Periplasmic Domain of Sensor Histidine Kinase CitA== |
| - | <StructureSection load='2v9a' size='340' side='right' caption='[[2v9a]], [[Resolution|resolution]] 2.00Å' scene=''> | + | <StructureSection load='2v9a' size='340' side='right'caption='[[2v9a]], [[Resolution|resolution]] 2.00Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2v9a]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_pneumoniae"_(schroeter_1886)_flugge_1886 "bacillus pneumoniae" (schroeter 1886) flugge 1886]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2V9A OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2V9A FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2v9a]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Klebsiella_pneumoniae Klebsiella pneumoniae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2V9A OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2V9A FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1p0z|1p0z]], [[2j80|2j80]]</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]] 2Å</td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Histidine_kinase Histidine kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.13.3 2.7.13.3] </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=2v9a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2v9a OCA], [https://pdbe.org/2v9a PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2v9a RCSB], [https://www.ebi.ac.uk/pdbsum/2v9a PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2v9a ProSAT]</span></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=2v9a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2v9a OCA], [http://pdbe.org/2v9a PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2v9a RCSB], [http://www.ebi.ac.uk/pdbsum/2v9a PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2v9a ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/CITA_KLEPN CITA_KLEPN] Member of the two-component regulatory system CitA/CitB. Probably activates CitB by phosphorylation. The periplasmic domain binds H-citrate(2-), which is essential for induction of the citrate-fermentation genes.<ref>PMID:10447894</ref> |
| | == 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: Histidine kinase]] | + | [[Category: Klebsiella pneumoniae]] |
| - | [[Category: Becker, S]] | + | [[Category: Large Structures]] |
| - | [[Category: Bott, M]] | + | [[Category: Becker S]] |
| - | [[Category: Griesinger, C]] | + | [[Category: Bott M]] |
| - | [[Category: Madden, D R]] | + | [[Category: Griesinger C]] |
| - | [[Category: Reinelt, S]] | + | [[Category: Madden DR]] |
| - | [[Category: Sevvana, M]] | + | [[Category: Reinelt S]] |
| - | [[Category: Sheldrick, G M]] | + | [[Category: Sevvana M]] |
| - | [[Category: Vijayan, V]] | + | [[Category: Sheldrick GM]] |
| - | [[Category: Zweckstetter, M]] | + | [[Category: Vijayan V]] |
| - | [[Category: Cita]]
| + | [[Category: Zweckstetter M]] |
| - | [[Category: Inner membrane]]
| + | |
| - | [[Category: Kinase]]
| + | |
| - | [[Category: Membrane]]
| + | |
| - | [[Category: Phosphorylation]]
| + | |
| - | [[Category: Sensor domain]]
| + | |
| - | [[Category: Sensor histidine kinase]]
| + | |
| - | [[Category: Signal transduction]]
| + | |
| - | [[Category: Transferase]]
| + | |
| - | [[Category: Transmembrane]]
| + | |
| - | [[Category: Two-component regulatory system]]
| + | |
| Structural highlights
Function
CITA_KLEPN Member of the two-component regulatory system CitA/CitB. Probably activates CitB by phosphorylation. The periplasmic domain binds H-citrate(2-), which is essential for induction of the citrate-fermentation genes.[1]
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
Sensor histidine kinases of two-component signal-transduction systems are essential for bacteria to adapt to variable environmental conditions. However, despite their prevalence, it is not well understood how extracellular signals such as ligand binding regulate the activity of these sensor kinases. CitA is the sensor histidine kinase in Klebsiella pneumoniae that regulates the transport and anaerobic metabolism of citrate in response to its extracellular concentration. We report here the X-ray structures of the periplasmic sensor domain of CitA in the citrate-free and citrate-bound states. A comparison of the two structures shows that ligand binding causes a considerable contraction of the sensor domain. This contraction may represent the molecular switch that activates transmembrane signaling in the receptor.
A ligand-induced switch in the periplasmic domain of sensor histidine kinase CitA.,Sevvana M, Vijayan V, Zweckstetter M, Reinelt S, Madden DR, Herbst-Irmer R, Sheldrick GM, Bott M, Griesinger C, Becker S J Mol Biol. 2008 Mar 21;377(2):512-23. Epub 2008 Jan 16. PMID:18258261[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Kaspar S, Perozzo R, Reinelt S, Meyer M, Pfister K, Scapozza L, Bott M. The periplasmic domain of the histidine autokinase CitA functions as a highly specific citrate receptor. Mol Microbiol. 1999 Aug;33(4):858-72. PMID:10447894
- ↑ Sevvana M, Vijayan V, Zweckstetter M, Reinelt S, Madden DR, Herbst-Irmer R, Sheldrick GM, Bott M, Griesinger C, Becker S. A ligand-induced switch in the periplasmic domain of sensor histidine kinase CitA. J Mol Biol. 2008 Mar 21;377(2):512-23. Epub 2008 Jan 16. PMID:18258261 doi:10.1016/j.jmb.2008.01.024
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