View source for 4kwe


==GDP-bound, double-stranded, curved FtsZ protofilament structure==
<StructureSection load='4kwe' size='340' side='right'caption='[[4kwe]], [[Resolution|resolution]] 2.91&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4kwe]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Mycobacterium_tuberculosis Mycobacterium tuberculosis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4KWE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4KWE FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GDP:GUANOSINE-5-DIPHOSPHATE'>GDP</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=4kwe FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4kwe OCA], [https://pdbe.org/4kwe PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4kwe RCSB], [https://www.ebi.ac.uk/pdbsum/4kwe PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4kwe ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/FTSZ_MYCTU FTSZ_MYCTU] Essential cell division protein that forms a contractile ring structure (Z ring) at the future cell division site. The regulation of the ring assembly controls the timing and the location of cell division. One of the functions of the FtsZ ring is to recruit other cell division proteins to the septum to produce a new cell wall between the dividing cells (By similarity). Binds GTP and shows GTPase activity.[HAMAP-Rule:MF_00909]
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== Publication Abstract from PubMed ==
The essential bacterial protein FtsZ is a guanosine triphosphatase that self-assembles into a structure at the division site termed the "Z ring". During cytokinesis, the Z ring exerts a constrictive force on the membrane by using the chemical energy of guanosine triphosphate hydrolysis. However, the structural basis of this constriction remains unresolved. Here, we present the crystal structure of a guanosine diphosphate-bound Mycobacterium tuberculosis FtsZ protofilament, which exhibits a curved conformational state. The structure reveals a longitudinal interface that is important for function. The protofilament curvature highlights a hydrolysis-dependent conformational switch at the T3 loop that leads to longitudinal bending between subunits, which could generate sufficient force to drive cytokinesis.

FtsZ protofilaments use a hinge-opening mechanism for constrictive force generation.,Li Y, Hsin J, Zhao L, Cheng Y, Shang W, Huang KC, Wang HW, Ye S Science. 2013 Jul 26;341(6144):392-5. doi: 10.1126/science.1239248. PMID:23888039<ref>PMID:23888039</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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<div class="pdbe-citations 4kwe" style="background-color:#fffaf0;"></div>

==See Also==
*[[Cell division protein 3D structures|Cell division protein 3D structures]]
*[[Proteins from Mycobacterium tuberculosis|Proteins from Mycobacterium tuberculosis]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Mycobacterium tuberculosis]]
[[Category: Cheng Y]]
[[Category: Hsin J]]
[[Category: Huang KC]]
[[Category: Li Y]]
[[Category: Shang W]]
[[Category: Wang HW]]
[[Category: Ye S]]
[[Category: Zhao L]]