Structure of the full-length HPr kinase/phosphatase from Staphylococcus xylosus at 1.95 A resolution: Mimicking the product/substrate of the phospho transfer reactions.
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Dynamic dissociating homo-oligomers and the control of protein functionBacterial tyrosine kinases: evolution, biological function and structural insightsStructural Basis of Reversible Phosphorylation by Maize Pyruvate Orthophosphate Dikinase Regulatory ProteinX-ray structure of a bifunctional protein kinase in complex with its protein substrate HPrStructural analysis of the bacterial HPr kinase/phosphorylase V267F mutant gives insights into the allosteric regulation mechanism of this bifunctional enzymeCross-phosphorylation of bacterial serine/threonine and tyrosine protein kinases on key regulatory residuesProperties and regulation of the bifunctional enzyme HPr kinase/phosphatase in Bacillus subtilis.Pyrophosphate-producing protein dephosphorylation by HPr kinase/phosphorylase: a relic of early life?Ser/Thr/Tyr protein phosphorylation in bacteria - for long time neglected, now well established.CcpA-dependent carbon catabolite repression in bacteria.How phosphotransferase system-related protein phosphorylation regulates carbohydrate metabolism in bacteriaThe phosphotransferase system of Lactobacillus casei: regulation of carbon metabolism and connection to cold shock response.Phylotype Dynamics of Bacterial P Utilization Genes in Microbialites and Bacterioplankton of a Monomictic Endorheic Lake.HPr kinase/phosphorylase, the sensor enzyme of catabolite repression in Gram-positive bacteria: structural aspects of the enzyme and the complex with its protein substrateHigh-resolution structure of the histidine-containing phosphocarrier protein (HPr) from Staphylococcus aureus and characterization of its interaction with the bifunctional HPr kinase/phosphorylase.In vivo activity of enzymatic and regulatory components of the phosphoenolpyruvate:sugar phosphotransferase system in Mycoplasma pneumoniaeMycoplasma pneumoniae HPr kinase/phosphorylase.Evolutionary relationship between the bacterial HPr kinase and the ubiquitous PEP-carboxykinase: expanding the P-loop nucleotidyl transferase superfamily
P2860
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P2860
Structure of the full-length HPr kinase/phosphatase from Staphylococcus xylosus at 1.95 A resolution: Mimicking the product/substrate of the phospho transfer reactions.
description
2002 nî lūn-bûn
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2002 թուականի Մարտին հրատարակուած գիտական յօդուած
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2002 թվականի մարտին հրատարակված գիտական հոդված
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2002年の論文
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2002年論文
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2002年論文
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2002年論文
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2002年論文
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2002年論文
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2002年论文
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name
Structure of the full-length H ...... the phospho transfer reactions
@nl
Structure of the full-length H ...... he phospho transfer reactions.
@ast
Structure of the full-length H ...... he phospho transfer reactions.
@en
Structure of the full-length H ...... he phospho transfer reactions.
@en-gb
type
label
Structure of the full-length H ...... the phospho transfer reactions
@nl
Structure of the full-length H ...... he phospho transfer reactions.
@ast
Structure of the full-length H ...... he phospho transfer reactions.
@en
Structure of the full-length H ...... he phospho transfer reactions.
@en-gb
altLabel
Structure of the full-length H ...... the phospho transfer reactions
@en
prefLabel
Structure of the full-length H ...... the phospho transfer reactions
@nl
Structure of the full-length H ...... he phospho transfer reactions.
@ast
Structure of the full-length H ...... he phospho transfer reactions.
@en
Structure of the full-length H ...... he phospho transfer reactions.
@en-gb
P2093
P2860
P50
P356
P1476
Structure of the full-length H ...... he phospho transfer reactions.
@en
P2093
Brigitte Koch
Jose Antonio Márquez
Klaus Scheffzek
Sonia Fieulaine
Sonja Hasenbein
Wolfgang Hengstenberg
P2860
P304
P356
10.1073/PNAS.052461499
P407
P577
2002-03-01T00:00:00Z