3m6m

<StructureSection load='3m6m' size='340' side='right' caption='[[3m6m]], [[Resolution|resolution]] 2.50&Aring;' scene=''>

<table><tr><td colspan='2'>[[3m6m]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/Xanthomonas_campestris_pv._campestris Xanthomonas campestris pv. campestris]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3M6M OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3M6M FirstGlance]. <br>

</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=IOD:IODIDE+ION'>IOD</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>

<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3m6n|3m6n]]</td></tr>

<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">rpfF, XCC1857 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=340 Xanthomonas campestris pv. campestris]), rpfC, XCC1856 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=340 Xanthomonas campestris pv. campestris])</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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3m6m FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3m6m OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3m6m RCSB], [http://www.ebi.ac.uk/pdbsum/3m6m PDBsum]</span></td></tr>

[[http://www.uniprot.org/uniprot/RPFC_XANCP RPFC_XANCP]] Member of the two-component regulatory system RpfG/RpfC, which is required for full virulence and for formation and dispersal of biofilms. Involved in sensing and responding to the diffusible signaling factor (DSF), which is essential for cell-cell signaling. RpfC is probably a sensor of environmental signals, including DSF, which is autophosphorylated at a histidine residue in response to the signal. Then, probably activates RpfG via a four-step phosphorelay. May also negatively regulate the production of DSF, independently of RpfG (By similarity).

<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/m6/3m6m_consurf.spt"</scriptWhenChecked>

</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/chain_selection.php?pdb_ID=2ata ConSurf].

<div style="background-color:#fffaf0;">

== Publication Abstract from PubMed ==

The diffusible signal factor (DSF)-dependent quorum sensing (QS) system adopts a novel protein-protein interaction mechanism to autoregulate the production of signal DSF. Here, we present the crystal structures of DSF synthase RpfF and its complex with the REC domain of sensor protein RpfC. RpfF is structurally similarity to the members of the crotonase superfamily and contains an N-terminal alpha/beta spiral core domain and a C-terminal alpha-helical region. Further structural and mutational analysis identified two catalytic glutamate residues, which is the conserved feature of the enoyl-CoA hydratases/dehydratases. A putative substrate-binding pocket was unveiled and the key roles of the residues implicated in substrate binding were verified by mutational analysis. The binding of the REC domain may lock RpfF in an inactive conformation by blocking the entrance of substrate binding pocket, thereby negatively regulating DSF production. These findings provide a structural model for the RpfC-RpfF interaction-mediated QS autoinduction mechanism.

Structural basis of the sensor-synthase interaction in autoinduction of the quorum sensing signal DSF biosynthesis.,Cheng Z, He YW, Lim SC, Qamra R, Walsh MA, Zhang LH, Song H Structure. 2010 Sep 8;18(9):1199-209. PMID:20826346<ref>PMID:20826346</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

</div>

*[[Response regulator|Response regulator]]

[[Category: Histidine kinase]]

[[Category: Cheng, Z]]

[[Category: Lim, S C]]

[[Category: Qamra, R]]

[[Category: Song, H]]

[[Category: Rpff]]