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| | ==Crystal Structure of RapH complexed with Spo0F== | | ==Crystal Structure of RapH complexed with Spo0F== |
| - | <StructureSection load='3q15' size='340' side='right' caption='[[3q15]], [[Resolution|resolution]] 2.19Å' scene=''> | + | <StructureSection load='3q15' size='340' side='right'caption='[[3q15]], [[Resolution|resolution]] 2.19Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3q15]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_globigii"_migula_1900 "bacillus globigii" migula 1900]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3Q15 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3Q15 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3q15]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/"vibrio_subtilis"_ehrenberg_1835 "vibrio subtilis" ehrenberg 1835]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3Q15 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3Q15 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | + | </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>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">BSU06830, rapH, yeeH, yzqA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1423 "Bacillus globigii" Migula 1900]), BSU37130, spo0F ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1423 "Bacillus globigii" Migula 1900])</td></tr> | + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">BSU06830, rapH, yeeH, yzqA ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1423 "Vibrio subtilis" Ehrenberg 1835]), BSU37130, spo0F ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1423 "Vibrio subtilis" Ehrenberg 1835])</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=3q15 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3q15 OCA], [http://pdbe.org/3q15 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3q15 RCSB], [http://www.ebi.ac.uk/pdbsum/3q15 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3q15 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=3q15 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3q15 OCA], [https://pdbe.org/3q15 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3q15 RCSB], [https://www.ebi.ac.uk/pdbsum/3q15 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3q15 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/SP0F_BACSU SP0F_BACSU]] Key element in the phosphorelay regulating sporulation initiation. Phosphorylation of spo0B during sporulation initiation. | + | [[https://www.uniprot.org/uniprot/SP0F_BACSU SP0F_BACSU]] Key element in the phosphorelay regulating sporulation initiation. Phosphorylation of spo0B during sporulation initiation. |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | ==See Also== | | ==See Also== |
| - | *[[Phosphotransferase|Phosphotransferase]] | + | *[[Phosphotransferase 3D structures|Phosphotransferase 3D structures]] |
| - | *[[Response regulator|Response regulator]] | + | *[[Response regulator 3D structure|Response regulator 3D structure]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Bacillus globigii migula 1900]] | + | [[Category: Vibrio subtilis ehrenberg 1835]] |
| | + | [[Category: Large Structures]] |
| | [[Category: Neiditch, M B]] | | [[Category: Neiditch, M B]] |
| | [[Category: Parashar, V]] | | [[Category: Parashar, V]] |
| Structural highlights
3q15 is a 4 chain structure with sequence from "vibrio_subtilis"_ehrenberg_1835 "vibrio subtilis" ehrenberg 1835. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
| | Ligands: | , , |
| Gene: | BSU06830, rapH, yeeH, yzqA ("Vibrio subtilis" Ehrenberg 1835), BSU37130, spo0F ("Vibrio subtilis" Ehrenberg 1835) |
| Resources: | FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT |
Function
[SP0F_BACSU] Key element in the phosphorelay regulating sporulation initiation. Phosphorylation of spo0B during sporulation initiation.
Publication Abstract from PubMed
Bacterial Rap family proteins have been most extensively studied in Bacillus subtilis, where they regulate activities including sporulation, genetic competence, antibiotic expression, and the movement of the ICEBs1 transposon. One subset of Rap proteins consists of phosphatases that control B. subtilis and B. anthracis sporulation by dephosphorylating the response regulator Spo0F. The mechanistic basis of Rap phosphatase activity was unknown. Here we present the RapH-Spo0F X-ray crystal structure, which shows that Rap proteins consist of a 3-helix bundle and a tetratricopeptide repeat domain. Extensive biochemical and genetic functional studies reveal the importance of the observed RapH-Spo0F interactions, including the catalytic role of a glutamine in the RapH 3-helix bundle that inserts into the Spo0F active site. We show that in addition to dephosphorylating Spo0F, RapH can antagonize sporulation by sterically blocking phosphoryl transfer to and from Spo0F. Our structure-function analysis of the RapH-Spo0F interaction identified Rap protein residues critical for Spo0F phosphatase activity. This information enabled us to assign Spo0F phosphatase activity to a Rap protein based on sequence alone, which was not previously possible. Finally, as the ultimate test of our newfound understanding of the structural requirements for Rap phosphatase function, a non-phosphatase Rap protein that inhibits the binding of the response regulator ComA to DNA was rationally engineered to dephosphorylate Spo0F. In addition to revealing the mechanistic basis of response regulator dephosphorylation by Rap proteins, our studies support the previously proposed T-loop-Y allostery model of receiver domain regulation that restricts the aromatic "switch" residue to an internal position when the beta4-alpha4 loop adopts an active-site proximal conformation.
Structural basis of response regulator dephosphorylation by Rap phosphatases.,Parashar V, Mirouze N, Dubnau DA, Neiditch MB PLoS Biol. 2011 Feb 8;9(2):e1000589. PMID:21346797[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Parashar V, Mirouze N, Dubnau DA, Neiditch MB. Structural basis of response regulator dephosphorylation by Rap phosphatases. PLoS Biol. 2011 Feb 8;9(2):e1000589. PMID:21346797 doi:10.1371/journal.pbio.1000589
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