1p0z: Difference between revisions

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<StructureSection load='1p0z' size='340' side='right'caption='[[1p0z]], [[Resolution|resolution]] 1.60&Aring;' scene=''>
<StructureSection load='1p0z' size='340' side='right'caption='[[1p0z]], [[Resolution|resolution]] 1.60&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1p0z]] is a 10 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=1P0Z OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1P0Z FirstGlance]. <br>
<table><tr><td colspan='2'>[[1p0z]] is a 10 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=1P0Z OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1P0Z FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FLC:CITRATE+ANION'>FLC</scene>, <scene name='pdbligand=MO7:BIS(MU4-OXO)-BIS(MU3-OXO)-OCTAKIS(MU2-OXO)-DODECAOXO-HEPTAMOLYBDENUM+(VI)'>MO7</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=OMO:MO(VI)(=O)(OH)2+CLUSTER'>OMO</scene></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]] 1.6&#8491;</td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">CITA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=573 "Bacillus pneumoniae" (Schroeter 1886) Flugge 1886])</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FLC:CITRATE+ANION'>FLC</scene>, <scene name='pdbligand=MO7:BIS(MU4-OXO)-BIS(MU3-OXO)-OCTAKIS(MU2-OXO)-DODECAOXO-HEPTAMOLYBDENUM+(VI)'>MO7</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=OMO:MO(VI)(=O)(OH)2+CLUSTER'>OMO</scene></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=1p0z FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1p0z OCA], [https://pdbe.org/1p0z PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1p0z RCSB], [https://www.ebi.ac.uk/pdbsum/1p0z PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1p0z ProSAT]</span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=1p0z FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1p0z OCA], [http://pdbe.org/1p0z PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1p0z RCSB], [http://www.ebi.ac.uk/pdbsum/1p0z PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1p0z ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://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>
[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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</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=1p0z ConSurf].
</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=1p0z ConSurf].
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<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The integral membrane sensor kinase CitA of Klebsiella pneumoniae is part of a two-component signal transduction system that regulates the transport and metabolism of citrate in response to its environmental concentration. Two-component systems are widely used by bacteria for such adaptive processes, but the stereochemistry of periplasmic ligand binding and the mechanism of signal transduction across the membrane remain poorly understood. The crystal structure of the CitAP periplasmic sensor domain in complex with citrate reveals a PAS fold, a versatile ligand-binding structural motif that has not previously been observed outside the cytoplasm or implicated in the transduction of conformational signals across the membrane. Citrate is bound in a pocket that is shared among many PAS domains but that shows structural variation according to the nature of the bound ligand. In CitAP, some of the citrate contact residues are located in the final strand of the central beta-sheet, which is connected to the C-terminal transmembrane helix. These secondary structure elements thus provide a potential conformational link between the periplasmic ligand binding site and the cytoplasmic signaling domains of the receptor.
The structure of the periplasmic ligand-binding domain of the sensor kinase CitA reveals the first extracellular PAS domain.,Reinelt S, Hofmann E, Gerharz T, Bott M, Madden DR J Biol Chem. 2003 Oct 3;278(40):39189-96. Epub 2003 Jul 16. PMID:12867417<ref>PMID:12867417</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1p0z" style="background-color:#fffaf0;"></div>
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Histidine kinase]]
[[Category: Klebsiella pneumoniae]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Bott, M]]
[[Category: Bott M]]
[[Category: Gerharz, T]]
[[Category: Gerharz T]]
[[Category: Hofmann, E]]
[[Category: Hofmann E]]
[[Category: Madden, D R]]
[[Category: Madden DR]]
[[Category: Reinelt, S]]
[[Category: Reinelt S]]
[[Category: Kinase]]
[[Category: Transferase]]
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