4czm

C. crescentus MreB, monomeric, AMPPNP

spinqualitylabelsall models 4czm, resolution 2.20Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4czm is a 2 chain structure with sequence from Caulobacter vibrioides. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.2Å Ligands: ANP, MG Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function 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] 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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