Crystal structure of a phosphatase-resistant mutant of sporulation response regulator Spo0F from Bacillus subtilis
about
Crystallographic and biochemical studies of DivK reveal novel features of an essential response regulator in Caulobacter crescentusCrystal Structures of the Response Regulator DosR from Mycobacterium tuberculosis Suggest a Helix Rearrangement Mechanism for Phosphorylation ActivationStructural basis for methylesterase CheB regulation by a phosphorylation-activated domainInteraction fidelity in two-component signaling.Multiple mechanisms of action for inhibitors of histidine protein kinases from bacterial two-component systems.Conformational changes of Spo0F along the phosphotransfer pathway.Cell cycle-dependent adaptor complex for ClpXP-mediated proteolysis directly integrates phosphorylation and second messenger signalsThe crystal structure of beryllofluoride Spo0F in complex with the phosphotransferase Spo0B represents a phosphotransfer pretransition stateAltered recognition mutants of the response regulator PhoB: a new genetic strategy for studying protein-protein interactions.Crystal structure of the inactive state of the receiver domain of Spo0A from Paenisporosarcina sp. TG-14, a psychrophilic bacterium isolated from an Antarctic glacier.Efficient spore synthesis in Bacillus subtilis depends on the CcdA protein.Structural insights into the function of the core-circadian factor TIMING OF CAB2 EXPRESSION 1 (TOC1).Topological frustration in beta alpha-repeat proteins: sequence diversity modulates the conserved folding mechanisms of alpha/beta/alpha sandwich proteins.Predominantly buried residues in the response regulator Spo0F influence specific sensor kinase recognitionSequence-, structure-, and dynamics-based comparisons of structurally homologous CheY-like proteins.Acid stress in the food pathogen Bacillus cereus.Interaction surface of the Spo0A response regulator with the Spo0E phosphatase.Purification and preliminary crystallographic studies on the sporulation response regulatory phosphotransferase protein, Spo0B, from Bacillus subtilis.The H box-harboring domain is key to the function of the Salmonella enterica PhoQ Mg2+-sensor in the recognition of its partner PhoP.A computational analysis on the specificity of interactions between histidine kinases and response regulators.GsmR, a response regulator with an HD-related output domain in Xanthomonas campestris, is positively controlled by Clp and is involved in the expression of genes responsible for flagellum synthesis.New insights into the interaction between the quorum-sensing receptor NprR and its DNA target, or the response regulator Spo0F.Structural characterization of Spo0E-like protein-aspartic acid phosphatases that regulate sporulation in bacilli.
P2860
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P2860
Crystal structure of a phosphatase-resistant mutant of sporulation response regulator Spo0F from Bacillus subtilis
description
1996 nî lūn-bûn
@nan
1996 թուականի Յունիսին հրատարակուած գիտական յօդուած
@hyw
1996 թվականի հունիսին հրատարակված գիտական հոդված
@hy
1996年の論文
@ja
1996年論文
@yue
1996年論文
@zh-hant
1996年論文
@zh-hk
1996年論文
@zh-mo
1996年論文
@zh-tw
1996年论文
@wuu
name
Crystal structure of a phospha ...... r Spo0F from Bacillus subtilis
@ast
Crystal structure of a phospha ...... r Spo0F from Bacillus subtilis
@en
Crystal structure of a phospha ...... r Spo0F from Bacillus subtilis
@nl
type
label
Crystal structure of a phospha ...... r Spo0F from Bacillus subtilis
@ast
Crystal structure of a phospha ...... r Spo0F from Bacillus subtilis
@en
Crystal structure of a phospha ...... r Spo0F from Bacillus subtilis
@nl
prefLabel
Crystal structure of a phospha ...... r Spo0F from Bacillus subtilis
@ast
Crystal structure of a phospha ...... r Spo0F from Bacillus subtilis
@en
Crystal structure of a phospha ...... r Spo0F from Bacillus subtilis
@nl
P2093
P1433
P1476
Crystal structure of a phospha ...... r Spo0F from Bacillus subtilis
@en
P2093
P304
P356
10.1016/S0969-2126(96)00074-3
P577
1996-06-15T00:00:00Z