View source for 4czi


==C. crescentus MreB, single filament, empty==
<StructureSection load='4czi' size='340' side='right'caption='[[4czi]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4czi]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Caulobacter_vibrioides Caulobacter vibrioides]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4CZI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4CZI FirstGlance]. <br>
</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=4czi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4czi OCA], [https://pdbe.org/4czi PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4czi RCSB], [https://www.ebi.ac.uk/pdbsum/4czi PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4czi ProSAT]</span></td></tr>
</table>
== Function ==
[[https://www.uniprot.org/uniprot/MREB_CAUVN MREB_CAUVN]] Forms membrane-associated dynamic filaments that are essential for cell shape determination (PubMed:14982627, PubMed:17880425, PubMed:24843005). Acts by regulating cell wall synthesis and cell elongation, and thus cell shape (PubMed:14982627, PubMed:17880425). A feedback loop between cell geometry and MreB localization may maintain elongated cell shape by targeting cell wall growth to regions of negative cell wall curvature (By similarity). Required for mid-cell peptidoglycan synthesis and cell division. Directs the localization of the cytosolic peptidoglycan precursor-synthesizing enzyme MurG (PubMed:17880425). Also required for proper chromosome segregation (PubMed:15707892). Directs the segregation of origin-proximal but not origin-distal loci (PubMed:15707892).[UniProtKB:P0A9X4]<ref>PMID:14982627</ref> <ref>PMID:15707892</ref> <ref>PMID:17880425</ref> <ref>PMID:24843005</ref> <ref>PMID:14982627</ref> 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Filaments of all actin-like proteins known to date are assembled from pairs of protofilaments that are arranged in a parallel fashion, generating polarity. Here we show that the prokaryotic actin homologue MreB forms pairs of protofilaments that adopt an antiparallel arrangement in vitro and in vivo. We provide an atomic view of antiparallel protofilaments of Caulobacter MreB as apparent from crystal structures. We show that a protofilament doublet is essential for MreB's function in cell shape maintenance and demonstrate by in vivo site-specific cross-linking the antiparallel orientation of MreB protofilaments in E. coli. 3D cryo-EM shows that pairs of protofilaments of Caulobacter MreB tightly bind to membranes. Crystal structures of different nucleotide and polymerisation states of Caulobacter MreB reveal conserved conformational changes accompanying antiparallel filament formation. Finally, the antimicrobial agents A22/MP265 are shown to bind close to the bound nucleotide of MreB, presumably preventing nucleotide hydrolysis and destabilising double protofilaments.

Bacterial actin MreB forms antiparallel double filaments.,Van den Ent F, Izore T, Bharat TA, Johnson CM, Lowe J Elife. 2014 May 2:e02634. doi: 10.7554/eLife.02634. PMID:24843005<ref>PMID:24843005</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4czi" style="background-color:#fffaf0;"></div>
== References ==
<references/>
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</StructureSection>
[[Category: Caulobacter vibrioides]]
[[Category: Large Structures]]
[[Category: Lowe J]]
[[Category: VandenEnt F]]