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| - | [[Image:3uz0.png|left|200px]] | |
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| - | <!-- | + | ==Crystal Structure of SpoIIIAH and SpoIIQ Complex== |
| - | The line below this paragraph, containing "STRUCTURE_3uz0", creates the "Structure Box" on the page.
| + | <StructureSection load='3uz0' size='340' side='right'caption='[[3uz0]], [[Resolution|resolution]] 2.82Å' scene=''> |
| - | You may change the PDB parameter (which sets the PDB file loaded into the applet)
| + | == Structural highlights == |
| - | or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
| + | <table><tr><td colspan='2'>[[3uz0]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_subtilis_subsp._subtilis_str._JH642 Bacillus subtilis subsp. subtilis str. JH642]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3UZ0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3UZ0 FirstGlance]. <br> |
| - | or leave the SCENE parameter empty for the default display.
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.82Å</td></tr> |
| - | --> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> |
| - | {{STRUCTURE_3uz0| PDB=3uz0 | SCENE= }}
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3uz0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3uz0 OCA], [https://pdbe.org/3uz0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3uz0 RCSB], [https://www.ebi.ac.uk/pdbsum/3uz0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3uz0 ProSAT]</span></td></tr> |
| | + | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/SP3AH_BACSU SP3AH_BACSU] Involved in forespore engulfment. Forms a channel with SpoIIIAH that is open on the forespore end and closed (or gated) on the mother cell end. This allows sigma-E-directed gene expression in the mother-cell compartment of the sporangium to trigger the activation of sigma-G forespore-specific gene expression by a pathway of intercellular signaling.<ref>PMID:15574594</ref> <ref>PMID:15752199</ref> <ref>PMID:16164552</ref> <ref>PMID:16959571</ref> <ref>PMID:17824930</ref> <ref>PMID:18485064</ref> <ref>PMID:18812514</ref> |
| | + | <div style="background-color:#fffaf0;"> |
| | + | == Publication Abstract from PubMed == |
| | + | Proteins SpoIIQ and SpoIIIAH interact through two membranes to connect the forespore and the mother cell during endospore development in the bacterium Bacillus subtilis. SpoIIIAH consists of a transmembrane segment and an extracellular domain with similarity to YscJ proteins. YscJ proteins form large multimeric rings that are the structural scaffolds for the assembly of type III secretion systems in Gram-negative bacteria. The predicted ring-forming motif of SpoIIIAH and other evidence led to the model that SpoIIQ and SpoIIIAH form the core components of a channel or transporter through which the mother cell nurtures forespore development. Therefore, to understand the roles of SpoIIIAH and SpoIIQ in channel formation, it is critical to determine whether SpoIIIAH adopts a ring-forming structural motif, and whether interaction of SpoIIIAH with SpoIIQ would preclude ring formation. We report a 2.8-A resolution structure of a complex of SpoIIQ and SpoIIIAH. SpoIIIAH folds into the ring-building structural motif, and modeling shows that the structure of the SpoIIQ-SpoIIIAH complex is compatible with forming a symmetrical oligomer that is similar to those in type III systems. The inner diameters of the two most likely ring models are large enough to accommodate several copies of other integral membrane proteins. SpoIIQ contains a LytM domain, which is found in metalloendopeptidases, but lacks residues important for metalloprotease activity. Other LytM domains appear to be involved in protein-protein interactions. We found that the LytM domain of SpoIIQ contains an accessory region that interacts with SpoIIIAH. |
| | | | |
| - | ===Crystal Structure of SpoIIIAH and SpoIIQ Complex===
| + | Structure of the basal components of a bacterial transporter.,Meisner J, Maehigashi T, Andre I, Dunham CM, Moran CP Jr Proc Natl Acad Sci U S A. 2012 Apr 3;109(14):5446-51. Epub 2012 Mar 19. PMID:22431613<ref>PMID:22431613</ref> |
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| - | | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> |
| - | <!--
| + | </div> |
| - | The line below this paragraph, {{ABSTRACT_PUBMED_22431613}}, adds the Publication Abstract to the page
| + | <div class="pdbe-citations 3uz0" style="background-color:#fffaf0;"></div> |
| - | (as it appears on PubMed at http://www.pubmed.gov), where 22431613 is the PubMed ID number.
| + | == References == |
| - | -->
| + | <references/> |
| - | {{ABSTRACT_PUBMED_22431613}}
| + | __TOC__ |
| - | | + | </StructureSection> |
| - | ==About this Structure== | + | [[Category: Bacillus subtilis subsp. subtilis str. JH642]] |
| - | [[3uz0]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3UZ0 OCA].
| + | [[Category: Large Structures]] |
| - | | + | [[Category: Dunham CM]] |
| - | ==Reference== | + | [[Category: Maehigashi T]] |
| - | <ref group="xtra">PMID:022431613</ref><references group="xtra"/> | + | [[Category: Meisner J]] |
| - | [[Category: Bacillus subtilis]] | + | |
| - | [[Category: Dunham, C M.]]
| + | |
| - | [[Category: Maehigashi, T.]]
| + | |
| - | [[Category: Meisner, J.]] | + | |
| - | [[Category: Hybrid transporter]] | + | |
| - | [[Category: Membrane]] | + | |
| - | [[Category: Sporulation]] | + | |
| - | [[Category: Transport protein]]
| + | |
| Structural highlights
Function
SP3AH_BACSU Involved in forespore engulfment. Forms a channel with SpoIIIAH that is open on the forespore end and closed (or gated) on the mother cell end. This allows sigma-E-directed gene expression in the mother-cell compartment of the sporangium to trigger the activation of sigma-G forespore-specific gene expression by a pathway of intercellular signaling.[1] [2] [3] [4] [5] [6] [7]
Publication Abstract from PubMed
Proteins SpoIIQ and SpoIIIAH interact through two membranes to connect the forespore and the mother cell during endospore development in the bacterium Bacillus subtilis. SpoIIIAH consists of a transmembrane segment and an extracellular domain with similarity to YscJ proteins. YscJ proteins form large multimeric rings that are the structural scaffolds for the assembly of type III secretion systems in Gram-negative bacteria. The predicted ring-forming motif of SpoIIIAH and other evidence led to the model that SpoIIQ and SpoIIIAH form the core components of a channel or transporter through which the mother cell nurtures forespore development. Therefore, to understand the roles of SpoIIIAH and SpoIIQ in channel formation, it is critical to determine whether SpoIIIAH adopts a ring-forming structural motif, and whether interaction of SpoIIIAH with SpoIIQ would preclude ring formation. We report a 2.8-A resolution structure of a complex of SpoIIQ and SpoIIIAH. SpoIIIAH folds into the ring-building structural motif, and modeling shows that the structure of the SpoIIQ-SpoIIIAH complex is compatible with forming a symmetrical oligomer that is similar to those in type III systems. The inner diameters of the two most likely ring models are large enough to accommodate several copies of other integral membrane proteins. SpoIIQ contains a LytM domain, which is found in metalloendopeptidases, but lacks residues important for metalloprotease activity. Other LytM domains appear to be involved in protein-protein interactions. We found that the LytM domain of SpoIIQ contains an accessory region that interacts with SpoIIIAH.
Structure of the basal components of a bacterial transporter.,Meisner J, Maehigashi T, Andre I, Dunham CM, Moran CP Jr Proc Natl Acad Sci U S A. 2012 Apr 3;109(14):5446-51. Epub 2012 Mar 19. PMID:22431613[8]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Blaylock B, Jiang X, Rubio A, Moran CP Jr, Pogliano K. Zipper-like interaction between proteins in adjacent daughter cells mediates protein localization. Genes Dev. 2004 Dec 1;18(23):2916-28. PMID:15574594 doi:http://dx.doi.org/10.1101/gad.1252704
- ↑ Doan T, Marquis KA, Rudner DZ. Subcellular localization of a sporulation membrane protein is achieved through a network of interactions along and across the septum. Mol Microbiol. 2005 Mar;55(6):1767-81. PMID:15752199 doi:http://dx.doi.org/10.1111/j.1365-2958.2005.04501.x
- ↑ Jiang X, Rubio A, Chiba S, Pogliano K. Engulfment-regulated proteolysis of SpoIIQ: evidence that dual checkpoints control sigma activity. Mol Microbiol. 2005 Oct;58(1):102-15. PMID:16164552 doi:http://dx.doi.org/MMI4811
- ↑ Broder DH, Pogliano K. Forespore engulfment mediated by a ratchet-like mechanism. Cell. 2006 Sep 8;126(5):917-28. PMID:16959571 doi:http://dx.doi.org/10.1016/j.cell.2006.06.053
- ↑ Aung S, Shum J, Abanes-De Mello A, Broder DH, Fredlund-Gutierrez J, Chiba S, Pogliano K. Dual localization pathways for the engulfment proteins during Bacillus subtilis sporulation. Mol Microbiol. 2007 Sep;65(6):1534-46. PMID:17824930 doi:http://dx.doi.org/MMI5887
- ↑ Camp AH, Losick R. A novel pathway of intercellular signalling in Bacillus subtilis involves a protein with similarity to a component of type III secretion channels. Mol Microbiol. 2008 Jul;69(2):402-17. doi: 10.1111/j.1365-2958.2008.06289.x. PMID:18485064 doi:http://dx.doi.org/10.1111/j.1365-2958.2008.06289.x
- ↑ Meisner J, Wang X, Serrano M, Henriques AO, Moran CP Jr. A channel connecting the mother cell and forespore during bacterial endospore formation. Proc Natl Acad Sci U S A. 2008 Sep 30;105(39):15100-5. doi:, 10.1073/pnas.0806301105. Epub 2008 Sep 23. PMID:18812514 doi:http://dx.doi.org/10.1073/pnas.0806301105
- ↑ Meisner J, Maehigashi T, Andre I, Dunham CM, Moran CP Jr. Structure of the basal components of a bacterial transporter. Proc Natl Acad Sci U S A. 2012 Apr 3;109(14):5446-51. Epub 2012 Mar 19. PMID:22431613 doi:10.1073/pnas.1120113109
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