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| - | ==DIVIVA N-TERMINAL DOMAIN== | + | ==DivIVA N-terminal domain== |
| - | <StructureSection load='2wuj' size='340' side='right' caption='[[2wuj]], [[Resolution|resolution]] 1.40Å' scene=''> | + | <StructureSection load='2wuj' size='340' side='right'caption='[[2wuj]], [[Resolution|resolution]] 1.40Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2wuj]] is a 2 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=2WUJ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2WUJ FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2wuj]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2WUJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2WUJ FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2wuk|2wuk]]</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]] 1.4Å</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=2wuj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2wuj OCA], [http://pdbe.org/2wuj PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2wuj RCSB], [http://www.ebi.ac.uk/pdbsum/2wuj PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2wuj 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=2wuj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2wuj OCA], [https://pdbe.org/2wuj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2wuj RCSB], [https://www.ebi.ac.uk/pdbsum/2wuj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2wuj ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/DIV4A_BACSU DIV4A_BACSU]] May act as a pilot protein, directing MinCD to the polar septation sites or by inhibiting MinCD at the midcell site of division. Required for polar localization of the chromosome during sporulation.<ref>PMID:9045828</ref> <ref>PMID:9219999</ref> | + | [https://www.uniprot.org/uniprot/DIV4A_BACSU DIV4A_BACSU] May act as a pilot protein, directing MinCD to the polar septation sites or by inhibiting MinCD at the midcell site of division. Required for polar localization of the chromosome during sporulation.<ref>PMID:9045828</ref> <ref>PMID:9219999</ref> |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
| | Check<jmol> | | Check<jmol> |
| | <jmolCheckbox> | | <jmolCheckbox> |
| - | <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/wu/2wuj_consurf.spt"</scriptWhenChecked> | + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/wu/2wuj_consurf.spt"</scriptWhenChecked> |
| | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> |
| | <text>to colour the structure by Evolutionary Conservation</text> | | <text>to colour the structure by Evolutionary Conservation</text> |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Bacillus globigii migula 1900]] | + | [[Category: Bacillus subtilis]] |
| - | [[Category: Leonard, T A]] | + | [[Category: Large Structures]] |
| - | [[Category: Lowe, J]] | + | [[Category: Leonard TA]] |
| - | [[Category: Oliva, M A]] | + | [[Category: Lowe J]] |
| - | [[Category: Bacterial cell division]] | + | [[Category: Oliva MA]] |
| - | [[Category: Cell cycle]]
| + | |
| - | [[Category: Septation]]
| + | |
| - | [[Category: Sporulation]]
| + | |
| Structural highlights
Function
DIV4A_BACSU May act as a pilot protein, directing MinCD to the polar septation sites or by inhibiting MinCD at the midcell site of division. Required for polar localization of the chromosome during sporulation.[1] [2]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
DivIVA is a conserved protein in Gram-positive bacteria that localizes at the poles and division sites, presumably through direct sensing of membrane curvature. DivIVA functions as a scaffold and is vital for septum site selection during vegetative growth and chromosome anchoring during sporulation. DivIVA deletion causes filamentous growth in Bacillus subtilis, whereas overexpression causes hyphal branching in Streptomyces coelicolor. We have determined the crystal structure of the N-terminal (Nt) domain of DivIVA, and show that it forms a parallel coiled-coil. It is capped with two unique crossed and intertwined loops, exposing hydrophobic and positively charged residues that we show here are essential for membrane binding. An intragenic suppressor introducing a positive charge restores membrane binding after mutating the hydrophobic residues. We propose that the hydrophobic residues insert into the membrane and that the positively charged residues bind to the membrane surface. A low-resolution crystal structure of the C-terminal (Ct) domain displays a curved tetramer made from two parallel coiled-coils. The Nt and Ct parts were then merged into a model of the full length, 30 nm long DivIVA protein.
Features critical for membrane binding revealed by DivIVA crystal structure.,Oliva MA, Halbedel S, Freund SM, Dutow P, Leonard TA, Veprintsev DB, Hamoen LW, Lowe J EMBO J. 2010 Jun 16;29(12):1988-2001. Epub 2010 May 25. PMID:20502438[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Cha JH, Stewart GC. The divIVA minicell locus of Bacillus subtilis. J Bacteriol. 1997 Mar;179(5):1671-83. PMID:9045828
- ↑ Edwards DH, Errington J. The Bacillus subtilis DivIVA protein targets to the division septum and controls the site specificity of cell division. Mol Microbiol. 1997 Jun;24(5):905-15. PMID:9219999
- ↑ Oliva MA, Halbedel S, Freund SM, Dutow P, Leonard TA, Veprintsev DB, Hamoen LW, Lowe J. Features critical for membrane binding revealed by DivIVA crystal structure. EMBO J. 2010 Jun 16;29(12):1988-2001. Epub 2010 May 25. PMID:20502438 doi:10.1038/emboj.2010.99
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