GlnK, a PII-homologue: structure reveals ATP binding site and indicates how the T-loops may be involved in molecular recognition
about
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 channelX-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 domainStructural basis for the regulation of N-acetylglutamate kinase by PII in Arabidopsis thalianaStructure of putative CutA1 fromHomo sapiensdetermined at 2.05 Å resolutionCrystal structures of the apo and ATP bound Mycobacterium tuberculosis nitrogen regulatory PII proteinMechanism of 2-oxoglutarate signaling by the Synechococcus elongatus PII signal transduction proteinStructural Basis and Target-specific Modulation of ADP Sensing by the Synechococcus elongatus PII Signaling ProteinAn engineered PII protein variant that senses a novel ligand: atomic resolution structure of the complex with citrateThe structure of a PII signaling protein from a halophilic archaeon reveals novel traits and high-salt adaptationsAdenylylation of mycobacterial Glnk (PII) protein is induced by nitrogen limitationSensory properties of the PII signalling protein family.Effects 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 perspectiveComplex structure and biochemical characterization of the Staphylococcus aureus cyclic diadenylate monophosphate (c-di-AMP)-binding protein PstA, the founding member of a new signal transduction protein family.The GlnD and GlnK homologues of Streptomyces coelicolor A3(2) are functionally dissimilar to their nitrogen regulatory system counterparts from enteric bacteria.Ammonia switch-off of nitrogen fixation in the methanogenic archaeon Methanococcus maripaludis: mechanistic features and requirement for the novel GlnB homologues, NifI(1) and NifI(2)Ternary complex formation between AmtB, GlnZ and the nitrogenase regulatory enzyme DraG reveals a novel facet of nitrogen regulation in bacteria.P(II) signal transduction proteins, pivotal players in microbial nitrogen controlMacromolecular intelligence in microorganisms.Crystal structure of the archaeal ammonium transporter Amt-1 from Archaeoglobus fulgidusElectron and atomic force microscopy of the trimeric ammonium transporter AmtB.In vitro analysis of the Escherichia coli AmtB-GlnK complex reveals a stoichiometric interaction and sensitivity to ATP and 2-oxoglutarate.Genetics of nitrogen regulation in Methanococcus maripaludisThe Amt/Mep/Rh family of ammonium transport proteins.The Escherichia coli signal transducers PII (GlnB) and GlnK form heterotrimers in vivo: fine tuning the nitrogen signal cascade.Molecular basis for the recognition of cyclic-di-AMP by PstA, a PII-like signal transduction protein.Identification of critical residues in GlnB for its activation of NifA activity in the photosynthetic bacterium Rhodospirillum rubrum.P(II) signal transduction proteins are ATPases whose activity is regulated by 2-oxoglutarate.Nitrogen regulation of protein-protein interactions and transcript levels of GlnK PII regulator and AmtB ammonium transporter homologs in Archaea.PII, the key regulator of nitrogen metabolism in the cyanobacteria.The role of effector molecules in signal transduction by PII proteins.P(II) signal transduction proteins: nitrogen regulation and beyond.From cyanobacteria to plants: conservation of PII functions during plastid evolution.Membrane sequestration of the signal transduction protein GlnK by the ammonium transporter AmtB.
P2860
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P2860
GlnK, a PII-homologue: structure reveals ATP binding site and indicates how the T-loops may be involved in molecular recognition
description
1998 nî lūn-bûn
@nan
1998 թուականի Սեպտեմբերին հրատարակուած գիտական յօդուած
@hyw
1998 թվականի սեպտեմբերին հրատարակված գիտական հոդված
@hy
1998年の論文
@ja
1998年論文
@yue
1998年論文
@zh-hant
1998年論文
@zh-hk
1998年論文
@zh-mo
1998年論文
@zh-tw
1998年论文
@wuu
name
GlnK, a PII-homologue: structu ...... olved in molecular recognition
@ast
GlnK, a PII-homologue: structu ...... olved in molecular recognition
@en
GlnK, a PII-homologue: structu ...... olved in molecular recognition
@nl
type
label
GlnK, a PII-homologue: structu ...... olved in molecular recognition
@ast
GlnK, a PII-homologue: structu ...... olved in molecular recognition
@en
GlnK, a PII-homologue: structu ...... olved in molecular recognition
@nl
prefLabel
GlnK, a PII-homologue: structu ...... olved in molecular recognition
@ast
GlnK, a PII-homologue: structu ...... olved in molecular recognition
@en
GlnK, a PII-homologue: structu ...... olved in molecular recognition
@nl
P2093
P356
P1476
GlnK, a PII-homologue: structu ...... olved in molecular recognition
@en
P2093
H V Westerhoff
S G Vasudevan
W C van Heeswijk
P304
P356
10.1006/JMBI.1998.1979
P407
P577
1998-09-11T00:00:00Z