Crystal structure of the bacterial cell division inhibitor MinC.
about
Dynamic assembly of MinD on phospholipid vesicles regulated by ATP and MinERecruitment of MinC, an inhibitor of Z-ring formation, to the membrane in Escherichia coli: role of MinD and MinE.Crystal structure of Helicobacter pylori MinE, a cell division topological specificity factorDetermination of the structure of the MinD-ATP complex reveals the orientation of MinD on the membrane and the relative location of the binding sites for MinE and MinCCrystal structure of the N-terminal domain of MinC dimerized via domain swappingGenetic and biochemical characterization of the MinC-FtsZ interaction in Bacillus subtilisMapping out Min protein patterns in fully confined fluidic chambersFtsZ in bacterial cytokinesis: cytoskeleton and force generator all in one.MinCDE exploits the dynamic nature of FtsZ filaments for its spatial regulationAsymmetric constriction of dividing Escherichia coli cells induced by expression of a fusion between two min proteins.Cytokinesis in bacteriaCharacterization of ftsZ mutations that render Bacillus subtilis resistant to MinCMinC mutants deficient in MinD- and DicB-mediated cell division inhibition due to loss of interaction with MinD, DicB, or a septal component.Essential biological processes of an emerging pathogen: DNA replication, transcription, and cell division in Acinetobacter sppThe dimerization function of MinC resides in a structurally autonomous C-terminal domainZipA is required for targeting of DMinC/DicB, but not DMinC/MinD, complexes to septal ring assemblies in Escherichia coliAsymmetric division and differential gene expression during a bacterial developmental program requires DivIVA.Divided we stand: splitting synthetic cells for their proliferationFtsA mutants impaired for self-interaction bypass ZipA suggesting a model in which FtsA's self-interaction competes with its ability to recruit downstream division proteins.Reconstitution of self-organizing protein gradients as spatial cues in cell-free systemsThe C-terminal domain of MinC inhibits assembly of the Z ring in Escherichia coli.Evidence That Bacteriophage λ Kil Peptide Inhibits Bacterial Cell Division by Disrupting FtsZ Protofilaments and Sequestering Protein Subunits.The switch I and II regions of MinD are required for binding and activating MinC.The crystal structure of a novel SAM-dependent methyltransferase PH1915 from Pyrococcus horikoshii.Dimerization or oligomerization of the actin-like FtsA protein enhances the integrity of the cytokinetic Z ring.Bacillus subtilis MinC destabilizes FtsZ-rings at new cell poles and contributes to the timing of cell division.The conserved C-terminal tail of FtsZ is required for the septal localization and division inhibitory activity of MinC(C)/MinD.Conserved glycines in the C terminus of MinC proteins are implicated in their functionality as cell division inhibitors.Spatial control of the cell division site by the Min system in Escherichia coli.Toward Spatially Regulated Division of Protocells: Insights into the E. coli Min System from in Vitro Studies.The keepers of the ring: regulators of FtsZ assembly.FtsZ-ring Architecture and Its Control by MinCD.Targeting of (D)MinC/MinD and (D)MinC/DicB complexes to septal rings in Escherichia coli suggests a multistep mechanism for MinC-mediated destruction of nascent FtsZ rings.ATP-dependent interactions between Escherichia coli Min proteins and the phospholipid membrane in vitro.Characterization of C-terminal structure of MinC and its implication in evolution of bacterial cell division.MinC/MinD copolymers are not required for Min function.MinCD cell division proteins form alternating copolymeric cytomotive filaments.MinC protein shortens FtsZ protofilaments by preferentially interacting with GDP-bound subunitsA function of DivIVA in Listeria monocytogenes division site selection.Backbone and side chain NMR assignments for the N-terminal domain of the cell division regulator MinC from Bacillus subtilis.
P2860
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P2860
Crystal structure of the bacterial cell division inhibitor MinC.
description
2001 nî lūn-bûn
@nan
2001 թուականի Մայիսին հրատարակուած գիտական յօդուած
@hyw
2001 թվականի մայիսին հրատարակված գիտական հոդված
@hy
2001年の論文
@ja
2001年論文
@yue
2001年論文
@zh-hant
2001年論文
@zh-hk
2001年論文
@zh-mo
2001年論文
@zh-tw
2001年论文
@wuu
name
Crystal structure of the bacterial cell division inhibitor MinC
@nl
Crystal structure of the bacterial cell division inhibitor MinC.
@ast
Crystal structure of the bacterial cell division inhibitor MinC.
@en
type
label
Crystal structure of the bacterial cell division inhibitor MinC
@nl
Crystal structure of the bacterial cell division inhibitor MinC.
@ast
Crystal structure of the bacterial cell division inhibitor MinC.
@en
prefLabel
Crystal structure of the bacterial cell division inhibitor MinC
@nl
Crystal structure of the bacterial cell division inhibitor MinC.
@ast
Crystal structure of the bacterial cell division inhibitor MinC.
@en
P2093
P2860
P356
P1433
P1476
Crystal structure of the bacterial cell division inhibitor MinC.
@en
P2093
P2860
P304
P356
10.1093/EMBOJ/20.10.2454
P407
P577
2001-05-01T00:00:00Z