4a2a: Difference between revisions
No edit summary |
No edit summary |
||
| (3 intermediate revisions by the same user not shown) | |||
| Line 1: | Line 1: | ||
==Thermotoga maritima FtsA:FtsZ(336-351)== | ==Thermotoga maritima FtsA:FtsZ(336-351)== | ||
<StructureSection load='4a2a' size='340' side='right' caption='[[4a2a]], [[Resolution|resolution]] 1.80Å' scene=''> | <StructureSection load='4a2a' size='340' side='right'caption='[[4a2a]], [[Resolution|resolution]] 1.80Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4a2a]] is a 4 chain structure with sequence from [ | <table><tr><td colspan='2'>[[4a2a]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermotoga_maritima Thermotoga maritima]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4A2A OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4A2A FirstGlance]. <br> | ||
</td></tr><tr><td class="sblockLbl"><b>[[ | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.8Å</td></tr> | ||
<tr><td class="sblockLbl"><b>[[ | <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></td></tr> | ||
<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4a2a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4a2a OCA], [https://pdbe.org/4a2a PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4a2a RCSB], [https://www.ebi.ac.uk/pdbsum/4a2a PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4a2a ProSAT]</span></td></tr> | ||
<table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/Q9WZU0_THEMA Q9WZU0_THEMA] | |||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
| Line 13: | Line 16: | ||
FtsA forms actin-like protofilaments.,Szwedziak P, Wang Q, Freund SM, Lowe J EMBO J. 2012 Mar 30. doi: 10.1038/emboj.2012.76. PMID:22473211<ref>PMID:22473211</ref> | FtsA forms actin-like protofilaments.,Szwedziak P, Wang Q, Freund SM, Lowe J EMBO J. 2012 Mar 30. doi: 10.1038/emboj.2012.76. PMID:22473211<ref>PMID:22473211</ref> | ||
From | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | </div> | ||
<div class="pdbe-citations 4a2a" style="background-color:#fffaf0;"></div> | |||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | |||
[[Category: Thermotoga maritima]] | [[Category: Thermotoga maritima]] | ||
[[Category: Lowe | [[Category: Lowe J]] | ||
[[Category: Szwedziak | [[Category: Szwedziak P]] | ||
Latest revision as of 14:18, 20 December 2023
Thermotoga maritima FtsA:FtsZ(336-351)Thermotoga maritima FtsA:FtsZ(336-351)
Structural highlights
FunctionPublication Abstract from PubMedFtsA is an early component of the Z-ring, the structure that divides most bacteria, formed by tubulin-like FtsZ. FtsA belongs to the actin family of proteins, showing an unusual subdomain architecture. Here we reconstitute the tethering of FtsZ to the membrane via FtsA's C-terminal amphipathic helix in vitro using Thermotoga maritima proteins. A crystal structure of the FtsA:FtsZ interaction reveals 16 amino acids of the FtsZ tail bound to subdomain 2B of FtsA. The same structure and a second crystal form of FtsA reveal that FtsA forms actin-like protofilaments with a repeat of 48 A. The identical repeat is observed when FtsA is polymerized using a lipid monolayer surface and FtsAs from three organisms form polymers in cells when overexpressed, as observed by electron cryotomography. Mutants that disrupt polymerization also show an elongated cell division phenotype in a temperature-sensitive FtsA background, demonstrating the importance of filament formation for FtsA's function in the Z-ring. FtsA forms actin-like protofilaments.,Szwedziak P, Wang Q, Freund SM, Lowe J EMBO J. 2012 Mar 30. doi: 10.1038/emboj.2012.76. PMID:22473211[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
|
| ||||||||||||||||||