The catalytic domain of Escherichia coli Lon protease has a unique fold and a Ser-Lys dyad in the active site
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Mutations to a glycine loop in the catalytic site of human Lon changes its protease, peptidase and ATPase activitiesSingle-turnover kinetic experiments confirm the existence of high- and low-affinity ATPase sites in Escherichia coli Lon proteaseArmand-Frappier outstanding student award -- role of ATP-dependent proteases in antibiotic resistance and virulenceMultitasking in the mitochondrion by the ATP-dependent Lon proteaseEvolution and significance of the Lon gene family in Arabidopsis organelle biogenesis and energy metabolismCrystal structure of the VP4 protease from infectious pancreatic necrosis virus reveals the acyl-enzyme complex for an intermolecular self-cleavage reactionStructure of the catalytic domain of the human mitochondrial Lon protease: Proposed relation of oligomer formation and activityStructure of the N-terminal fragment ofEscherichia coliLon proteaseCrystal structure of Lon protease: molecular architecture of gated entry to a sequestered degradation chamberCrystal Structure of a Viral Protease Intramolecular Acyl-enzyme Complex: INSIGHTS INTO cis-CLEAVAGE AT THE VP4/VP3 JUNCTION OF TELLINA BIRNAVIRUSCrystal Structures of Yellowtail Ascites Virus VP4 Protease: TRAPPING AN INTERNAL CLEAVAGE SITE TRANS ACYL-ENZYME COMPLEX IN A NATIVE SER/LYS DYAD ACTIVE SITEStructures of an ATP-independent Lon-like protease and its complexes with covalent inhibitorsUnconventional serine proteases: variations on the catalytic Ser/His/Asp triad configurationEvidence that two ATP-dependent (Lon) proteases in Borrelia burgdorferi serve different functionsThe Lon protease is essential for full virulence in Pseudomonas aeruginosaProtein crystallography for non-crystallographers, or how to get the best (but not more) from published macromolecular structures.The N-terminal domain plays a crucial role in the structure of a full-length human mitochondrial Lon protease.The active site of a lon protease from Methanococcus jannaschii distinctly differs from the canonical catalytic Dyad of Lon proteases.Cleavage site selection within a folded substrate by the ATP-dependent lon protease.Protease gene families in Populus and Arabidopsis.Bacterial RadA is a DnaB-type helicase interacting with RecA to promote bidirectional D-loop extensionA Lon-like protease with no ATP-powered unfolding activityEndopeptidase activity characterization of E. coli-derived infectious bursal disease virus protein 4 tubules.Mitochondrial Lon protease at the crossroads of oxidative stress, ageing and cancer.Distinct quaternary structures of the AAA+ Lon protease control substrate degradation.CODAS syndrome is associated with mutations of LONP1, encoding mitochondrial AAA+ Lon protease.YoeB toxin is activated during thermal stress.Molecular machines for protein degradation.Lon protease of Azorhizobium caulinodans ORS571 is required for suppression of reb gene expression.Expression, purification and crystallization of a birnavirus-encoded protease, VP4, from blotched snakehead virus (BSNV).Purification, crystallization and preliminary X-ray analysis of truncated and mutant forms of VP4 protease from infectious pancreatic necrosis virusSelf-compartmentalized bacterial proteases and pathogenesis.Slicing a protease: structural features of the ATP-dependent Lon proteases gleaned from investigations of isolated domains.Crystal structure of the N-terminal domain of E. coli Lon protease.Identification of patterns in diffraction intensities affected by radiation exposureFunctional mechanics of the ATP-dependent Lon protease- lessons from endogenous protein and synthetic peptide substrates.A mutation in the N domain of Escherichia coli lon stabilizes dodecamers and selectively alters degradation of model substrates.Utilization of positional isotope exchange experiments to evaluate reversibility of ATP hydrolysis catalyzed by Escherichia coli Lon protease.An overview of molecular stress response mechanisms in Escherichia coli contributing to survival of Shiga toxin-producing Escherichia coli during raw milk cheese production.Natural substrates of plant proteases: how can protease degradomics extend our knowledge?
P2860
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P2860
The catalytic domain of Escherichia coli Lon protease has a unique fold and a Ser-Lys dyad in the active site
description
2004 nî lūn-bûn
@nan
2004 թուականի Փետրուարին հրատարակուած գիտական յօդուած
@hyw
2004 թվականի փետրվարին հրատարակված գիտական հոդված
@hy
2004年の論文
@ja
2004年論文
@yue
2004年論文
@zh-hant
2004年論文
@zh-hk
2004年論文
@zh-mo
2004年論文
@zh-tw
2004年论文
@wuu
name
The catalytic domain of Escher ...... er-Lys dyad in the active site
@ast
The catalytic domain of Escher ...... er-Lys dyad in the active site
@en
The catalytic domain of Escher ...... er-Lys dyad in the active site
@nl
type
label
The catalytic domain of Escher ...... er-Lys dyad in the active site
@ast
The catalytic domain of Escher ...... er-Lys dyad in the active site
@en
The catalytic domain of Escher ...... er-Lys dyad in the active site
@nl
prefLabel
The catalytic domain of Escher ...... er-Lys dyad in the active site
@ast
The catalytic domain of Escher ...... er-Lys dyad in the active site
@en
The catalytic domain of Escher ...... er-Lys dyad in the active site
@nl
P2093
P2860
P50
P3181
P356
P1476
The catalytic domain of Escher ...... er-Lys dyad in the active site
@en
P2093
Anna G Khalatova
Edward E Melnikov
Fatima Rasulova
Istvan Botos
Joseph E Tropea
Michael R Maurizi
Scott Cherry
Tatyana V Rotanova
P2860
P304
P3181
P356
10.1074/JBC.M312243200
P407
P577
2004-02-27T00:00:00Z