3tuf

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<StructureSection load='3tuf' size='340' side='right'caption='[[3tuf]], [[Resolution|resolution]] 2.26&Aring;' scene=''>
<StructureSection load='3tuf' size='340' side='right'caption='[[3tuf]], [[Resolution|resolution]] 2.26&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[3tuf]] is a 2 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=3TUF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3TUF FirstGlance]. <br>
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<table><tr><td colspan='2'>[[3tuf]] 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=3TUF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3TUF FirstGlance]. <br>
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</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">BSU36550, spoIIQ, ywnI ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1423 "Vibrio subtilis" Ehrenberg 1835]), BSU24360, spoIIIAH ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1423 "Vibrio subtilis" Ehrenberg 1835])</td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.26&#8491;</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=3tuf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3tuf OCA], [https://pdbe.org/3tuf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3tuf RCSB], [https://www.ebi.ac.uk/pdbsum/3tuf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3tuf 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=3tuf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3tuf OCA], [https://pdbe.org/3tuf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3tuf RCSB], [https://www.ebi.ac.uk/pdbsum/3tuf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3tuf ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[https://www.uniprot.org/uniprot/SP2Q_BACSU SP2Q_BACSU]] Involved in forespore engulfment and required for anchoring membrane proteins on the forespore side of the septal membrane. 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:9140963</ref> <ref>PMID:10781563</ref> <ref>PMID:15882622</ref> <ref>PMID:15752199</ref> <ref>PMID:16164552</ref> <ref>PMID:16959571</ref> <ref>PMID:17824930</ref> <ref>PMID:18077456</ref> <ref>PMID:18485064</ref> <ref>PMID:18812514</ref> [[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>
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[https://www.uniprot.org/uniprot/SP2Q_BACSU SP2Q_BACSU] Involved in forespore engulfment and required for anchoring membrane proteins on the forespore side of the septal membrane. 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:9140963</ref> <ref>PMID:10781563</ref> <ref>PMID:15882622</ref> <ref>PMID:15752199</ref> <ref>PMID:16164552</ref> <ref>PMID:16959571</ref> <ref>PMID:17824930</ref> <ref>PMID:18077456</ref> <ref>PMID:18485064</ref> <ref>PMID:18812514</ref>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Following asymmetric cell division during spore formation in Bacillus subtilis, a forespore expressed membrane protein SpoIIQ, interacts across an intercellular space with a mother cell-expressed membrane protein, SpoIIIAH. Their interaction can serve as a molecular "ratchet" contributing to the migration of the mother cell membrane around that of the forespore in a phagocytosis-like process termed engulfment. Upon completion of engulfment, SpoIIQ and SpoIIIAH are integral components of a recently proposed intercellular channel allowing passage from the mother cell into the forespore of factors required for late gene expression in this compartment. Here we show that the extracellular domains of SpoIIQ and SpoIIIAH form a heterodimeric complex in solution. The crystal structure of this complex reveals that SpoIIQ has a LytM-like zinc-metalloprotease fold but with an incomplete zinc coordination sphere and no metal. SpoIIIAH has an alpha-helical subdomain and a protruding beta-sheet subdomain, which mediates interactions with SpoIIQ. SpoIIIAH has sequence and structural homology to EscJ, a type III secretion system protein that forms a 24-fold symmetric ring. Superposition of the structures of SpoIIIAH and EscJ reveals that the SpoIIIAH protomer overlaps with two adjacent protomers of EscJ, allowing us to generate a dodecameric SpoIIIAH ring by using structural homology. Following this superposition, the SpoIIQ chains also form a closed dodecameric ring abutting the SpoIIIAH ring, producing an assembly surrounding a 60 A channel. The dimensions and organization of the proposed complex suggest it is a plausible model for the extracellular component of a gap junction-like intercellular channel.
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Structure of components of an intercellular channel complex in sporulating Bacillus subtilis.,Levdikov VM, Blagova EV, McFeat A, Fogg MJ, Wilson KS, Wilkinson AJ Proc Natl Acad Sci U S A. 2012 Apr 3;109(14):5441-5. Epub 2012 Mar 19. PMID:22431604<ref>PMID:22431604</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 3tuf" style="background-color:#fffaf0;"></div>
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== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Vibrio subtilis ehrenberg 1835]]
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[[Category: Bacillus subtilis]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Blagova, E V]]
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[[Category: Blagova EV]]
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[[Category: Levdikov, V M]]
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[[Category: Levdikov VM]]
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[[Category: Wilkinson, A J]]
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[[Category: Wilkinson AJ]]
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[[Category: Cell engulfment and signalling]]
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[[Category: Intercellular channel]]
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[[Category: Intercellular signalling]]
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[[Category: Intercellular space]]
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[[Category: Signaling protein]]
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[[Category: Sporulation]]
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Current revision

Structure of the SpoIIQ-SpoIIIAH pore forming complex.

PDB ID 3tuf

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