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| | ==Structural organization of FtsB, a transmembrane protein of the bacterial divisome== | | ==Structural organization of FtsB, a transmembrane protein of the bacterial divisome== |
| - | <StructureSection load='4iff' size='340' side='right' caption='[[4iff]], [[Resolution|resolution]] 2.30Å' scene=''> | + | <StructureSection load='4iff' size='340' side='right'caption='[[4iff]], [[Resolution|resolution]] 2.30Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4iff]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Bpph2 Bpph2]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4IFF OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4IFF FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4iff]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_virus_phi29 Bacillus virus phi29] and [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4IFF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4IFF 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='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='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">7 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10756 BPPH2])</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=4iff FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4iff OCA], [https://pdbe.org/4iff PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4iff RCSB], [https://www.ebi.ac.uk/pdbsum/4iff PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4iff 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=4iff FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4iff OCA], [http://pdbe.org/4iff PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4iff RCSB], [http://www.ebi.ac.uk/pdbsum/4iff PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4iff ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/FTSB_ECOLI FTSB_ECOLI] Essential cell division protein. May link together the upstream cell division proteins, which are predominantly cytoplasmic, with the downstream cell division proteins, which are predominantly periplasmic.[HAMAP-Rule:MF_00599]<ref>PMID:11972052</ref> <ref>PMID:19233928</ref> [https://www.uniprot.org/uniprot/SCAF_BPPH2 SCAF_BPPH2] Scaffolding protein involved in the icosahedric procapsid assembly. Coassembles with the capsid proteins to form the procapsid, in which the scaffolding protein is found within the external shell of icosahedrally arranged capsid protein subunits. In a subsequent step the scaffolding protein molecules are released from the procapsid.<ref>PMID:17098197</ref> <ref>PMID:17198713</ref> <ref>PMID:23896641</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: Bpph2]] | + | [[Category: Bacillus virus phi29]] |
| - | [[Category: Khadria, A]] | + | [[Category: Escherichia coli]] |
| - | [[Category: LaPointe, L M]] | + | [[Category: Large Structures]] |
| - | [[Category: Rayment, I]] | + | [[Category: Khadria A]] |
| - | [[Category: Senes, A]]
| + | [[Category: LaPointe LM]] |
| - | [[Category: Subramaniam, S]] | + | [[Category: Rayment I]] |
| - | [[Category: Taylor, K C]] | + | [[Category: Senes A]] |
| - | [[Category: Bacterial division]] | + | [[Category: Subramaniam S]] |
| - | [[Category: Cell cycle]] | + | [[Category: Taylor KC]] |
| - | [[Category: Ftsl]] | + | |
| Structural highlights
Function
FTSB_ECOLI Essential cell division protein. May link together the upstream cell division proteins, which are predominantly cytoplasmic, with the downstream cell division proteins, which are predominantly periplasmic.[HAMAP-Rule:MF_00599][1] [2] SCAF_BPPH2 Scaffolding protein involved in the icosahedric procapsid assembly. Coassembles with the capsid proteins to form the procapsid, in which the scaffolding protein is found within the external shell of icosahedrally arranged capsid protein subunits. In a subsequent step the scaffolding protein molecules are released from the procapsid.[3] [4] [5]
Publication Abstract from PubMed
We report the first structural analysis of an integral membrane protein of the bacterial divisome. FtsB is a single-pass membrane protein with a periplasmic coiled coil. Its heterologous association with its partner FtsL represents an essential event for the recruitment of the late components to the division site. Using a combination of mutagenesis, computational modeling, and X-ray crystallography, we determined that FtsB self-associates, and we investigated its structural organization. We found that the transmembrane domain of FtsB homo-oligomerizes through an evolutionarily conserved interaction interface where a polar residue (Gln 16) plays a critical role through the formation of an interhelical hydrogen bond. The crystal structure of the periplasmic domain, solved as a fusion with Gp7, shows that 30 juxta-membrane amino acids of FtsB form a canonical coiled coil. The presence of conserved Gly residue in the linker region suggests that flexibility between the transmembrane and coiled coil domains is functionally important. We hypothesize that the transmembrane helices of FtsB form a stable dimeric core for its association with FtsL into a higher-order oligomer and that FtsL is required to stabilize the periplasmic domain of FtsB, leading to the formation of a complex that is competent for binding to FtsQ, and to their consequent recruitment to the divisome. The study provides an experimentally validated structural model and identifies point mutations that disrupt association, thereby establishing important groundwork for the functional characterization of FtsB in vivo.
Structural Organization of FtsB, a Transmembrane Protein of the Bacterial Divisome.,Lapointe LM, Taylor KC, Subramaniam S, Khadria A, Rayment I, Senes A Biochemistry. 2013 Apr 4. PMID:23520975[6]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Buddelmeijer N, Judson N, Boyd D, Mekalanos JJ, Beckwith J. YgbQ, a cell division protein in Escherichia coli and Vibrio cholerae, localizes in codependent fashion with FtsL to the division site. Proc Natl Acad Sci U S A. 2002 Apr 30;99(9):6316-21. Epub 2002 Apr 23. PMID:11972052 doi:http://dx.doi.org/10.1073/pnas.092128499
- ↑ Gonzalez MD, Beckwith J. Divisome under construction: distinct domains of the small membrane protein FtsB are necessary for interaction with multiple cell division proteins. J Bacteriol. 2009 Apr;191(8):2815-25. doi: 10.1128/JB.01597-08. Epub 2009 Feb 20. PMID:19233928 doi:http://dx.doi.org/10.1128/JB.01597-08
- ↑ Choi KH, Morais MC, Anderson DL, Rossmann MG. Determinants of bacteriophage phi29 head morphology. Structure. 2006 Nov;14(11):1723-7. PMID:17098197 doi:http://dx.doi.org/10.1016/j.str.2006.09.007
- ↑ Fu CY, Morais MC, Battisti AJ, Rossmann MG, Prevelige PE Jr. Molecular dissection of o29 scaffolding protein function in an in vitro assembly system. J Mol Biol. 2007 Mar 2;366(4):1161-73. Epub 2006 Dec 6. PMID:17198713 doi:http://dx.doi.org/10.1016/j.jmb.2006.11.091
- ↑ Li R, Cherwa JE Jr, Prevelige PE Jr. varphi29 Scaffolding and connector structure-function relationship studied by trans-complementation. Virology. 2013 Sep;444(1-2):355-62. doi: 10.1016/j.virol.2013.07.001. Epub 2013, Jul 27. PMID:23896641 doi:http://dx.doi.org/10.1016/j.virol.2013.07.001
- ↑ Lapointe LM, Taylor KC, Subramaniam S, Khadria A, Rayment I, Senes A. Structural Organization of FtsB, a Transmembrane Protein of the Bacterial Divisome. Biochemistry. 2013 Apr 4. PMID:23520975 doi:10.1021/bi400222r
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