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Herbaspirillum seropedicae signal transduction protein PII is structurally similar to the enteric GlnKInhibitory 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 resolutionStructural basis for the regulation of N-acetylglutamate kinase by PII in Arabidopsis thalianaCrystal 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 structures of the CutA1 proteins fromThermus thermophilusandPyrococcus horikoshii: characterization of metal-binding sites and metal-induced assemblyNitrogen assimilation in Escherichia coli: putting molecular data into a systems perspectiveTernary complex formation between AmtB, GlnZ and the nitrogenase regulatory enzyme DraG reveals a novel facet of nitrogen regulation in bacteria.Crystal structure of the archaeal ammonium transporter Amt-1 from Archaeoglobus fulgidusIn 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.Regulation of nitrogenase by 2-oxoglutarate-reversible, direct binding of a PII-like nitrogen sensor protein to dinitrogenase.Genetic screen for regulatory mutations in Methanococcus maripaludis and its use in identification of induction-deficient mutants of the euryarchaeal repressor NrpRP(II) signal transduction proteins: nitrogen regulation and beyond.A PII-Like Protein Regulated by Bicarbonate: Structural and Biochemical Studies of the Carboxysome-Associated CPII Protein.PII T-loop mutations affecting signal transduction to NtrB also abolish yeast two-hybrid interactions.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.In vitro interactions between the PII proteins and the nitrogenase regulatory enzymes dinitrogenase reductase ADP-ribosyltransferase (DraT) and dinitrogenase reductase-activating glycohydrolase (DraG) in Azospirillum brasilense.The novel protein phosphatase PphA from Synechocystis PCC 6803 controls dephosphorylation of the signalling protein PII.Different responses of the GlnB and GlnZ proteins upon in vitro uridylylation by the Azospirillum brasilense GlnD protein.2-Oxoglutarate levels control adenosine nucleotide binding by Herbaspirillum seropedicae PII proteins.Interpreting the plastid carbon, nitrogen, and energy status. A role for PII?
P2860
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P2860
description
2001 nî lūn-bûn
@nan
2001年の論文
@ja
2001年学术文章
@wuu
2001年学术文章
@zh-cn
2001年学术文章
@zh-hans
2001年学术文章
@zh-my
2001年学术文章
@zh-sg
2001年學術文章
@yue
2001年學術文章
@zh
2001年學術文章
@zh-hant
name
The structure of the PII-ATP complex.
@en
The structure of the PII-ATP complex.
@nl
type
label
The structure of the PII-ATP complex.
@en
The structure of the PII-ATP complex.
@nl
prefLabel
The structure of the PII-ATP complex.
@en
The structure of the PII-ATP complex.
@nl
P2093
P2860
P1433
P1476
The structure of the PII-ATP complex.
@en
P2093
P2860
P304
P356
10.1046/J.1432-1327.2001.02074.X
P407
P50
P577
2001-04-01T00:00:00Z