4czk: Difference between revisions
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''' | ==C. crescentus MreB, single filament, AMPPNP, MP265 inhibitor== | ||
<StructureSection load='4czk' size='340' side='right' caption='[[4czk]], [[Resolution|resolution]] 2.60Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[4czk]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4CZK OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4CZK FirstGlance]. <br> | |||
</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ANP:PHOSPHOAMINOPHOSPHONIC+ACID-ADENYLATE+ESTER'>ANP</scene>, <scene name='pdbligand=F90:4-CHLOROBENZYL+CARBAMIMIDOTHIOATE'>F90</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene><br> | |||
<tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4cze|4cze]], [[4czf|4czf]], [[4czg|4czg]], [[4czh|4czh]], [[4czi|4czi]], [[4czj|4czj]], [[4czl|4czl]], [[4czm|4czm]]</td></tr> | |||
<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4czk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4czk OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4czk RCSB], [http://www.ebi.ac.uk/pdbsum/4czk PDBsum]</span></td></tr> | |||
<table> | |||
<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®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Ent, F van den.]] | |||
[[Category: Lowe, J.]] | |||
[[Category: Bacterial actin]] | |||
[[Category: Bacterial cytoskeleton]] | |||
[[Category: Structural protein]] | |||
Revision as of 11:48, 11 June 2014
C. crescentus MreB, single filament, AMPPNP, MP265 inhibitorC. crescentus MreB, single filament, AMPPNP, MP265 inhibitor
Structural highlights
Publication Abstract from PubMedFilaments 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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