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| | ==B. subtilis GpsB C-terminal Domain== | | ==B. subtilis GpsB C-terminal Domain== |
| - | <StructureSection load='5an5' size='340' side='right' caption='[[5an5]], [[Resolution|resolution]] 1.20Å' scene=''> | + | <StructureSection load='5an5' size='340' side='right'caption='[[5an5]], [[Resolution|resolution]] 1.20Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5an5]] is a 9 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5AN5 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5AN5 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5an5]] is a 9 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=5AN5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5AN5 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></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]] 1.2Å</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=5an5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5an5 OCA], [http://pdbe.org/5an5 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5an5 RCSB], [http://www.ebi.ac.uk/pdbsum/5an5 PDBsum]</span></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></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=5an5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5an5 OCA], [https://pdbe.org/5an5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5an5 RCSB], [https://www.ebi.ac.uk/pdbsum/5an5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5an5 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/GPSB_BACSU GPSB_BACSU]] Divisome component that associates with the complex late in its assembly, after the Z-ring is formed, and is dependent on DivIC and PBP2B for its recruitment to the divisome. Together with EzrA, is a key component of the system that regulates PBP1 localization during cell cycle progression. Its main role could be the removal of PBP1 from the cell pole after pole maturation is completed. Also contributes to the recruitment of PBP1 to the division complex. Not essential for septum formation.<ref>PMID:18363795</ref> <ref>PMID:18776011</ref> | + | [https://www.uniprot.org/uniprot/GPSB_BACSU GPSB_BACSU] Divisome component that associates with the complex late in its assembly, after the Z-ring is formed, and is dependent on DivIC and PBP2B for its recruitment to the divisome. Together with EzrA, is a key component of the system that regulates PBP1 localization during cell cycle progression. Its main role could be the removal of PBP1 from the cell pole after pole maturation is completed. Also contributes to the recruitment of PBP1 to the division complex. Not essential for septum formation.<ref>PMID:18363795</ref> <ref>PMID:18776011</ref> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Cleverley, R M]] | + | [[Category: Bacillus subtilis subsp. subtilis str. 168]] |
| - | [[Category: Grohennig, S]] | + | [[Category: Large Structures]] |
| - | [[Category: Hain, T]] | + | [[Category: Cleverley RM]] |
| - | [[Category: Halbedel, S]] | + | [[Category: Grohennig S]] |
| - | [[Category: Lane, H V]] | + | [[Category: Hain T]] |
| - | [[Category: Lewis, R J]] | + | [[Category: Halbedel S]] |
| - | [[Category: Mannala, G Krishna]] | + | [[Category: Krishna Mannala G]] |
| - | [[Category: Moller, L]] | + | [[Category: Lane HV]] |
| - | [[Category: Rismondo, J]] | + | [[Category: Lewis RJ]] |
| - | [[Category: Steglich, A]] | + | [[Category: Moller L]] |
| - | [[Category: Bacterial growth regulation]] | + | [[Category: Rismondo J]] |
| - | [[Category: Cell cycle]] | + | [[Category: Steglich A]] |
| - | [[Category: Cell division]]
| + | |
| - | [[Category: Cell wall synthesis]]
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| Structural highlights
Function
GPSB_BACSU Divisome component that associates with the complex late in its assembly, after the Z-ring is formed, and is dependent on DivIC and PBP2B for its recruitment to the divisome. Together with EzrA, is a key component of the system that regulates PBP1 localization during cell cycle progression. Its main role could be the removal of PBP1 from the cell pole after pole maturation is completed. Also contributes to the recruitment of PBP1 to the division complex. Not essential for septum formation.[1] [2]
Publication Abstract from PubMed
Each bacterium has to co-ordinate its growth with division to ensure genetic stability of the population. Consequently, cell division and growth are tightly-regulated phenomena, albeit different bacteria utilise one of several alternative regulatory mechanisms to maintain control. Here we consider GpsB, which is linked to cell growth and division in Gram-positive bacteria. DeltagpsB mutants of the human pathogen Listeria monocytogenes show severe lysis, division and growth defects due to distortions of cell wall biosynthesis. Consistent with this premise, GpsB interacts both in vitro and in vivo with the major bi-functional penicillin binding protein. We solved the crystal structure of GpsB and the interaction interfaces in both proteins are identified and validated. The inactivation of gpsB results in strongly attenuated virulence in animal experiments, comparable in degree to classical listerial virulence factor mutants. Therefore, GpsB is essential for in vitro and in vivo growth of a highly virulent food-borne pathogen, suggesting that GpsB could be a target for the future design of novel antibacterials.
Structure of the bacterial cell division determinant GpsB and its interaction with penicillin binding proteins.,Rismondo J, Cleverley RM, Lane HV, Grosshennig S, Steglich A, Moller L, Mannala GK, Hain T, Lewis RJ, Halbedel S Mol Microbiol. 2015 Nov 17. doi: 10.1111/mmi.13279. PMID:26575090[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Claessen D, Emmins R, Hamoen LW, Daniel RA, Errington J, Edwards DH. Control of the cell elongation-division cycle by shuttling of PBP1 protein in Bacillus subtilis. Mol Microbiol. 2008 May;68(4):1029-46. Epub 2008 Mar 19. PMID:18363795 doi:http://dx.doi.org/MMI6210
- ↑ Tavares JR, de Souza RF, Meira GL, Gueiros-Filho FJ. Cytological characterization of YpsB, a novel component of the Bacillus subtilis divisome. J Bacteriol. 2008 Nov;190(21):7096-107. doi: 10.1128/JB.00064-08. Epub 2008 Sep, 5. PMID:18776011 doi:http://dx.doi.org/10.1128/JB.00064-08
- ↑ Rismondo J, Cleverley RM, Lane HV, Grosshennig S, Steglich A, Moller L, Mannala GK, Hain T, Lewis RJ, Halbedel S. Structure of the bacterial cell division determinant GpsB and its interaction with penicillin binding proteins. Mol Microbiol. 2015 Nov 17. doi: 10.1111/mmi.13279. PMID:26575090 doi:http://dx.doi.org/10.1111/mmi.13279
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