Structure of the Escherichia coli signal transducing protein PII
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Herbaspirillum seropedicae signal transduction protein PII is structurally similar to the enteric GlnKCrystal structure of ATP phosphoribosyltransferase from Mycobacterium tuberculosisStructure of a conserved hypothetical protein SA1388 from S. aureus reveals a capped hexameric toroid with two PII domain lids and a dinuclear metal centerInhibitory complex of the transmembrane ammonia channel, AmtB, and the cytosolic regulatory protein, GlnK, at 1.96 AStructure of GlnK1 with bound effectors indicates regulatory mechanism for ammonia uptakeThe crystal structure of the Escherichia coli AmtB-GlnK complex reveals how GlnK regulates the ammonia channelThe evolutionarily conserved trimeric structure of CutA1 proteins suggests a role in signal transductionX-ray crystal structure of CutA from Thermotoga maritima at 1.4 Å resolutionThe 2.2 Å resolution crystal structure ofBacillus cereusNif3-family protein YqfO reveals a conserved dimetal-binding motif and a regulatory domainStructure of putative CutA1 fromHomo sapiensdetermined at 2.05 Å resolutionCrystal structures of the apo and ATP bound Mycobacterium tuberculosis nitrogen regulatory PII proteinAn engineered PII protein variant that senses a novel ligand: atomic resolution structure of the complex with citrateThe crystal structure of human glycosylation-inhibiting factor is a trimeric barrel with three 6-stranded beta-sheetsEffects of T-loop modification on the PII-signalling protein: structure of uridylylated Escherichia coli GlnB bound to ATP.Nitrogen assimilation in Escherichia coli: putting molecular data into a systems perspectiveExpression of glnB and a glnB-like gene (glnK) in a ribulose bisphosphate carboxylase/oxygenase-deficient mutant of Rhodobacter sphaeroidesPhysiological role for the GlnK protein of enteric bacteria: relief of NifL inhibition under nitrogen-limiting conditions.Azorhizobium caulinodans PII and GlnK proteins control nitrogen fixation and ammonia assimilationP(II) signal transduction proteins, pivotal players in microbial nitrogen controlIn vitro analysis of the Escherichia coli AmtB-GlnK complex reveals a stoichiometric interaction and sensitivity to ATP and 2-oxoglutarate.The Amt/Mep/Rh family of ammonium transport proteins.Coexistence of two structurally similar but functionally different PII proteins in Azospirillum brasilense.The Escherichia coli signal transducers PII (GlnB) and GlnK form heterotrimers in vivo: fine tuning the nitrogen signal cascade.Identification of critical residues in GlnB for its activation of NifA activity in the photosynthetic bacterium Rhodospirillum rubrum.PII, the key regulator of nitrogen metabolism in the cyanobacteria.P(II) signal transduction proteins: nitrogen regulation and beyond.From cyanobacteria to plants: conservation of PII functions during plastid evolution.The role of the T-loop of the signal transducing protein PII from Escherichia coli.Genetic and biochemical analysis of phosphatase activity of Escherichia coli NRII (NtrB) and its regulation by the PII signal transduction protein.Structure/function analysis of the PII signal transduction protein of Escherichia coli: genetic separation of interactions with protein receptors.Probing interactions of the homotrimeric PII signal transduction protein with its receptors by use of PII heterotrimers formed in vitro from wild-type and mutant subunitsNitrogen control in bacteria.Signal transduction to the Azotobacter vinelandii NIFL-NIFA regulatory system is influenced directly by interaction with 2-oxoglutarate and the PII regulatory protein.Identification of Rhodospirillum rubrum GlnB variants that are altered in their ability to interact with different targets in response to nitrogen status signals.Sensation and signaling of alpha-ketoglutarate and adenylylate energy charge by the Escherichia coli PII signal transduction protein require cooperation of the three ligand-binding sites within the PII trimer.Structure of the PII signal transduction protein of Neisseria meningitidis at 1.85 A resolution.The structure of the PII-ATP complex.Direct interaction of the NifL regulatory protein with the GlnK signal transducer enables the Azotobacter vinelandii NifL-NifA regulatory system to respond to conditions replete for nitrogen.Applying charge discrimination with electrospray ionization-mass spectrometry to protein analyses.Interpreting the plastid carbon, nitrogen, and energy status. A role for PII?
P2860
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P2860
Structure of the Escherichia coli signal transducing protein PII
description
1994 nî lūn-bûn
@nan
1994 թուականի Հոկտեմբերին հրատարակուած գիտական յօդուած
@hyw
1994 թվականի հոտեմբերին հրատարակված գիտական հոդված
@hy
1994年の論文
@ja
1994年論文
@yue
1994年論文
@zh-hant
1994年論文
@zh-hk
1994年論文
@zh-mo
1994年論文
@zh-tw
1994年论文
@wuu
name
Structure of the Escherichia coli signal transducing protein PII
@ast
Structure of the Escherichia coli signal transducing protein PII
@en
Structure of the Escherichia coli signal transducing protein PII
@nl
type
label
Structure of the Escherichia coli signal transducing protein PII
@ast
Structure of the Escherichia coli signal transducing protein PII
@en
Structure of the Escherichia coli signal transducing protein PII
@nl
prefLabel
Structure of the Escherichia coli signal transducing protein PII
@ast
Structure of the Escherichia coli signal transducing protein PII
@en
Structure of the Escherichia coli signal transducing protein PII
@nl
P2093
P1433
P1476
Structure of the Escherichia coli signal transducing protein PII
@en
P2093
P304
P356
10.1016/S0969-2126(94)00100-6
P577
1994-10-01T00:00:00Z