7q6d: Difference between revisions

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'''Unreleased structure'''


The entry 7q6d is ON HOLD
==E. coli FtsA 1-405 ATP 3 Ni==
<StructureSection load='7q6d' size='340' side='right'caption='[[7q6d]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[7q6d]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7Q6D OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7Q6D FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.8&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=NI:NICKEL+(II)+ION'>NI</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=7q6d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7q6d OCA], [https://pdbe.org/7q6d PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7q6d RCSB], [https://www.ebi.ac.uk/pdbsum/7q6d PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7q6d ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/FTSA_ECOLI FTSA_ECOLI] Essential cell division protein that assists in the assembly of the Z ring (PubMed:11847116). May serve as the principal membrane anchor for the Z ring (PubMed:15752196). Also required for the recruitment to the septal ring of the downstream cell division proteins FtsK, FtsQ, FtsL, FtsI and FtsN (PubMed:10027987, PubMed:24750258, PubMed:9282742, PubMed:9495771, PubMed:9603865, PubMed:9882666). Binds ATP (PubMed:11053380).<ref>PMID:10027987</ref> <ref>PMID:11053380</ref> <ref>PMID:11847116</ref> <ref>PMID:15752196</ref> <ref>PMID:24750258</ref> <ref>PMID:9282742</ref> <ref>PMID:9495771</ref> <ref>PMID:9603865</ref> <ref>PMID:9882666</ref>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
During bacterial cell division, filaments of tubulin-like FtsZ form the Z-ring, which is the cytoplasmic scaffold for divisome assembly. In Escherichia coli, the actin homologue FtsA anchors the Z-ring to the membrane and recruits divisome components, including bitopic FtsN. FtsN regulates the periplasmic peptidoglycan synthase FtsWI. To characterize how FtsA regulates FtsN, we applied electron microscopy to show that E. coli FtsA forms antiparallel double filaments on lipid monolayers when bound to the cytoplasmic tail of FtsN. Using X-ray crystallography, we demonstrate that Vibrio maritimus FtsA crystallizes as an equivalent double filament. We identified an FtsA-FtsN interaction site in the IA-IC interdomain cleft of FtsA using X-ray crystallography and confirmed that FtsA forms double filaments in vivo by site-specific cysteine cross-linking. FtsA-FtsN double filaments reconstituted in or on liposomes prefer negative Gaussian curvature, like those of MreB, the actin-like protein of the elongasome. We propose that curved antiparallel FtsA double filaments together with treadmilling FtsZ filaments organize septal peptidoglycan synthesis in the division plane.


Authors:  
Bacterial divisome protein FtsA forms curved antiparallel double filaments when binding to FtsN.,Nierhaus T, McLaughlin SH, Burmann F, Kureisaite-Ciziene D, Maslen SL, Skehel JM, Yu CWH, Freund SMV, Funke LFH, Chin JW, Lowe J Nat Microbiol. 2022 Oct;7(10):1686-1701. doi: 10.1038/s41564-022-01206-9. Epub , 2022 Sep 19. PMID:36123441<ref>PMID:36123441</ref>


Description:  
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
[[Category: Unreleased Structures]]
</div>
<div class="pdbe-citations 7q6d" style="background-color:#fffaf0;"></div>
 
==See Also==
*[[Cell division protein 3D structures|Cell division protein 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Escherichia coli K-12]]
[[Category: Large Structures]]
[[Category: Kureisaite-Ciziene D]]
[[Category: Lowe J]]
[[Category: Nierhaus T]]

Latest revision as of 12:33, 9 October 2024

E. coli FtsA 1-405 ATP 3 NiE. coli FtsA 1-405 ATP 3 Ni

Structural highlights

7q6d is a 1 chain structure with sequence from Escherichia coli K-12. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.8Å
Ligands:, ,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

FTSA_ECOLI Essential cell division protein that assists in the assembly of the Z ring (PubMed:11847116). May serve as the principal membrane anchor for the Z ring (PubMed:15752196). Also required for the recruitment to the septal ring of the downstream cell division proteins FtsK, FtsQ, FtsL, FtsI and FtsN (PubMed:10027987, PubMed:24750258, PubMed:9282742, PubMed:9495771, PubMed:9603865, PubMed:9882666). Binds ATP (PubMed:11053380).[1] [2] [3] [4] [5] [6] [7] [8] [9]

Publication Abstract from PubMed

During bacterial cell division, filaments of tubulin-like FtsZ form the Z-ring, which is the cytoplasmic scaffold for divisome assembly. In Escherichia coli, the actin homologue FtsA anchors the Z-ring to the membrane and recruits divisome components, including bitopic FtsN. FtsN regulates the periplasmic peptidoglycan synthase FtsWI. To characterize how FtsA regulates FtsN, we applied electron microscopy to show that E. coli FtsA forms antiparallel double filaments on lipid monolayers when bound to the cytoplasmic tail of FtsN. Using X-ray crystallography, we demonstrate that Vibrio maritimus FtsA crystallizes as an equivalent double filament. We identified an FtsA-FtsN interaction site in the IA-IC interdomain cleft of FtsA using X-ray crystallography and confirmed that FtsA forms double filaments in vivo by site-specific cysteine cross-linking. FtsA-FtsN double filaments reconstituted in or on liposomes prefer negative Gaussian curvature, like those of MreB, the actin-like protein of the elongasome. We propose that curved antiparallel FtsA double filaments together with treadmilling FtsZ filaments organize septal peptidoglycan synthesis in the division plane.

Bacterial divisome protein FtsA forms curved antiparallel double filaments when binding to FtsN.,Nierhaus T, McLaughlin SH, Burmann F, Kureisaite-Ciziene D, Maslen SL, Skehel JM, Yu CWH, Freund SMV, Funke LFH, Chin JW, Lowe J Nat Microbiol. 2022 Oct;7(10):1686-1701. doi: 10.1038/s41564-022-01206-9. Epub , 2022 Sep 19. PMID:36123441[10]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

See Also

References

  1. ↑ Ghigo JM, Weiss DS, Chen JC, Yarrow JC, Beckwith J. Localization of FtsL to the Escherichia coli septal ring. Mol Microbiol. 1999 Jan;31(2):725-37. doi: 10.1046/j.1365-2958.1999.01213.x. PMID:10027987 doi:http://dx.doi.org/10.1046/j.1365-2958.1999.01213.x
  2. ↑ Yim L, Vandenbussche G, Mingorance J, Rueda S, Casanova M, Ruysschaert JM, Vicente M. Role of the carboxy terminus of Escherichia coli FtsA in self-interaction and cell division. J Bacteriol. 2000 Nov;182(22):6366-73. doi: 10.1128/JB.182.22.6366-6373.2000. PMID:11053380 doi:http://dx.doi.org/10.1128/JB.182.22.6366-6373.2000
  3. ↑ Pichoff S, Lutkenhaus J. Unique and overlapping roles for ZipA and FtsA in septal ring assembly in Escherichia coli. EMBO J. 2002 Feb 15;21(4):685-93. doi: 10.1093/emboj/21.4.685. PMID:11847116 doi:http://dx.doi.org/10.1093/emboj/21.4.685
  4. ↑ Pichoff S, Lutkenhaus J. Tethering the Z ring to the membrane through a conserved membrane targeting sequence in FtsA. Mol Microbiol. 2005 Mar;55(6):1722-34. doi: 10.1111/j.1365-2958.2005.04522.x. PMID:15752196 doi:http://dx.doi.org/10.1111/j.1365-2958.2005.04522.x
  5. ↑ Busiek KK, Margolin W. A role for FtsA in SPOR-independent localization of the essential Escherichia coli cell division protein FtsN. Mol Microbiol. 2014 Jun;92(6):1212-26. doi: 10.1111/mmi.12623. Epub 2014 May 8. PMID:24750258 doi:http://dx.doi.org/10.1111/mmi.12623
  6. ↑ Addinall SG, Cao C, Lutkenhaus J. FtsN, a late recruit to the septum in Escherichia coli. Mol Microbiol. 1997 Jul;25(2):303-9. doi: 10.1046/j.1365-2958.1997.4641833.x. PMID:9282742 doi:http://dx.doi.org/10.1046/j.1365-2958.1997.4641833.x
  7. ↑ Yu XC, Tran AH, Sun Q, Margolin W. Localization of cell division protein FtsK to the Escherichia coli septum and identification of a potential N-terminal targeting domain. J Bacteriol. 1998 Mar;180(5):1296-304. doi: 10.1128/JB.180.5.1296-1304.1998. PMID:9495771 doi:http://dx.doi.org/10.1128/JB.180.5.1296-1304.1998
  8. ↑ Wang L, Khattar MK, Donachie WD, Lutkenhaus J. FtsI and FtsW are localized to the septum in Escherichia coli. J Bacteriol. 1998 Jun;180(11):2810-6. doi: 10.1128/JB.180.11.2810-2816.1998. PMID:9603865 doi:http://dx.doi.org/10.1128/JB.180.11.2810-2816.1998
  9. ↑ Chen JC, Weiss DS, Ghigo JM, Beckwith J. Septal localization of FtsQ, an essential cell division protein in Escherichia coli. J Bacteriol. 1999 Jan;181(2):521-30. PMID:9882666
  10. ↑ Nierhaus T, McLaughlin SH, Bürmann F, Kureisaite-Ciziene D, Maslen SL, Skehel JM, Yu CWH, Freund SMV, Funke LFH, Chin JW, Löwe J. Bacterial divisome protein FtsA forms curved antiparallel double filaments when binding to FtsN. Nat Microbiol. 2022 Oct;7(10):1686-1701. PMID:36123441 doi:10.1038/s41564-022-01206-9

7q6d, resolution 2.80Å

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