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| | ==Crystal structure of B. subtilis 168 GlpQ in complex with bicine== | | ==Crystal structure of B. subtilis 168 GlpQ in complex with bicine== |
| - | <StructureSection load='5t91' size='340' side='right' caption='[[5t91]], [[Resolution|resolution]] 1.53Å' scene=''> | + | <StructureSection load='5t91' size='340' side='right'caption='[[5t91]], [[Resolution|resolution]] 1.53Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5t91]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5T91 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5T91 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5t91]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_subtilis_subsp._subtilis_str._168 Bacillus subtilis subsp. subtilis str. 168]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5T91 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5T91 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BCN:BICINE'>BCN</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</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]] 1.53Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5t9b|5t9b]], [[5t9c|5t9c]]</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BCN:BICINE'>BCN</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Glycerophosphodiester_phosphodiesterase Glycerophosphodiester phosphodiesterase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.4.46 3.1.4.46] </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=5t91 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5t91 OCA], [https://pdbe.org/5t91 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5t91 RCSB], [https://www.ebi.ac.uk/pdbsum/5t91 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5t91 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=5t91 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5t91 OCA], [http://pdbe.org/5t91 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5t91 RCSB], [http://www.ebi.ac.uk/pdbsum/5t91 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5t91 ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/GLPQ_BACSU GLPQ_BACSU]] Glycerophosphoryl diester phosphodiesterase hydrolyzes deacylated phospholipids to G3P and the corresponding alcohols. | + | [https://www.uniprot.org/uniprot/GLPQ_BACSU GLPQ_BACSU] Glycerophosphoryl diester phosphodiesterase hydrolyzes deacylated phospholipids to G3P and the corresponding alcohols. |
| | <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== |
| - | *[[Phosphodiesterase|Phosphodiesterase]] | + | *[[Phosphodiesterase 3D structures|Phosphodiesterase 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Glycerophosphodiester phosphodiesterase]] | + | [[Category: Bacillus subtilis subsp. subtilis str. 168]] |
| - | [[Category: Li, F K.K]]
| + | [[Category: Large Structures]] |
| - | [[Category: Strynadka, N C.J]] | + | [[Category: Li FKK]] |
| - | [[Category: Hydrolase]] | + | [[Category: Strynadka NCJ]] |
| - | [[Category: Metal binding protein]] | + | |
| Structural highlights
Function
GLPQ_BACSU Glycerophosphoryl diester phosphodiesterase hydrolyzes deacylated phospholipids to G3P and the corresponding alcohols.
Publication Abstract from PubMed
The cell wall of most Gram-positive bacteria contains equal amounts of peptidoglycan and the phosphate-rich glycopolymer wall teichoic acid (WTA). During phosphate-limited growth of the Gram-positive model organism Bacillus subtilis 168, WTA is lost from the cell wall in a response mediated by the PhoPR two component system, which regulates genes involved in phosphate conservation and acquisition. It has been thought that WTA provides a phosphate source to sustain growth during starvation conditions, however, WTA degradative pathways have not been described for this, or any condition of bacterial growth. Here, we uncover roles for the Bacillus subtilis PhoP regulon genes glpQ and phoD as encoding secreted phosphodiesterases that function in WTA metabolism during phosphate starvation. Unlike the parent 168 strain, DeltaglpQ or DeltaphoD mutants retained WTA and ceased growth upon phosphate limitation. Characterization of GlpQ and PhoD enzymatic activities, in addition to X-ray crystal structures of GlpQ, revealed distinct mechanisms of WTA depolymerisation for the two enzymes - GlpQ catalyzes exolytic cleavage of individual monomer units, while PhoD catalyzes endo-hydrolysis at non-specific sites throughout the polymer. The combination of these activities appears requisite for the utilization of WTA as a phosphate reserve. Phenotypic characterization of the DeltaglpQ and DeltaphoD mutants revealed altered cell morphologies, and effects on autolytic activity and antibiotic susceptibilities that, unexpectedly, also occurred in phosphate-replete conditions. Our findings offer novel insight into the B. subtilis phosphate starvation response and implicate WTA hydrolase activity as a determinant of functional properties of the Gram-positive cell envelope.
Identification of two phosphate starvation-induced wall teichoic acid hydrolases provides first insights into the degradative pathway of a key bacterial cell wall component.,Myers CL, Li FK, Koo BM, El-Halfawy OM, French S, Gross CA, Strynadka NC, Brown ED J Biol Chem. 2016 Oct 25. pii: jbc.M116.760447. PMID:27780866[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Myers CL, Li FK, Koo BM, El-Halfawy OM, French S, Gross CA, Strynadka NC, Brown ED. Identification of two phosphate starvation-induced wall teichoic acid hydrolases provides first insights into the degradative pathway of a key bacterial cell wall component. J Biol Chem. 2016 Oct 25. pii: jbc.M116.760447. PMID:27780866 doi:http://dx.doi.org/10.1074/jbc.M116.760447
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