The catalytic domain of Escherichia coli Lon protease has a unique fold and a Ser-Lys dyad in the active site - Wikidata - awgldk - TriplyDB

The catalytic domain of Escherichia coli Lon protease has a unique fold and a Ser-Lys dyad in the active site

The catalytic domain of Escherichia coli Lon protease has a unique fold and a Ser-Lys dyad in the active site

http://www.wikidata.org/entity/Q27642758

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Mutations to a glycine loop in the catalytic site of human Lon changes its protease, peptidase and ATPase activities Single-turnover kinetic experiments confirm the existence of high- and low-affinity ATPase sites in Escherichia coli Lon protease Armand-Frappier outstanding student award -- role of ATP-dependent proteases in antibiotic resistance and virulence Multitasking in the mitochondrion by the ATP-dependent Lon protease Evolution and significance of the Lon gene family in Arabidopsis organelle biogenesis and energy metabolism Crystal structure of the VP4 protease from infectious pancreatic necrosis virus reveals the acyl-enzyme complex for an intermolecular self-cleavage reaction Structure of the catalytic domain of the human mitochondrial Lon protease: Proposed relation of oligomer formation and activity Structure of the N-terminal fragment ofEscherichia coliLon protease Crystal structure of Lon protease: molecular architecture of gated entry to a sequestered degradation chamber Crystal Structure of a Viral Protease Intramolecular Acyl-enzyme Complex: INSIGHTS INTO cis-CLEAVAGE AT THE VP4/VP3 JUNCTION OF TELLINA BIRNAVIRUS Crystal Structures of Yellowtail Ascites Virus VP4 Protease: TRAPPING AN INTERNAL CLEAVAGE SITE TRANS ACYL-ENZYME COMPLEX IN A NATIVE SER/LYS DYAD ACTIVE SITE Structures of an ATP-independent Lon-like protease and its complexes with covalent inhibitors Unconventional serine proteases: variations on the catalytic Ser/His/Asp triad configuration Evidence that two ATP-dependent (Lon) proteases in Borrelia burgdorferi serve different functions The Lon protease is essential for full virulence in Pseudomonas aeruginosa Protein 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 extension A Lon-like protease with no ATP-powered unfolding activity Endopeptidase 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 virus Self-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 exposure Functional 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?

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The catalytic domain of Escherichia coli Lon protease has a unique fold and a Ser-Lys dyad in the active site

http://www.wikidata.org/entity/Q27642758

description

2004 nî lūn-bûn

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2004 թուականի Փետրուարին հրատարակուած գիտական յօդուած

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2004 թվականի փետրվարին հրատարակված գիտական հոդված

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2004年の論文

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2004年論文

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2004年論文

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2004年論文

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2004年論文

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2004年論文

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2004年论文

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name

The catalytic domain of Escher ...... er-Lys dyad in the active site

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The catalytic domain of Escher ...... er-Lys dyad in the active site

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The catalytic domain of Escher ...... er-Lys dyad in the active site

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The catalytic domain of Escher ...... er-Lys dyad in the active site

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The catalytic domain of Escher ...... er-Lys dyad in the active site

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The catalytic domain of Escher ...... er-Lys dyad in the active site

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The catalytic domain of Escher ...... er-Lys dyad in the active site

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The catalytic domain of Escher ...... er-Lys dyad in the active site

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The catalytic domain of Escher ...... er-Lys dyad in the active site

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Journal of Biological Chemistry

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The catalytic domain of Escher ...... er-Lys dyad in the active site

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P2093

Anna G Khalatova

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Edward E Melnikov

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Fatima Rasulova

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Istvan Botos

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Joseph E Tropea

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Michael R Maurizi

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Scott Cherry

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Tatyana V Rotanova

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P2860

Crystallography & NMR System: A New Software Suite for Macromolecular Structure Determination

Processing of X-ray diffraction data collected in oscillation mode

Crystal structure of the lambda repressor C-terminal domain provides a model for cooperative operator binding

Carboxyl proteinase from Pseudomonas defines a novel family of subtilisin-like enzymes

Crystal structure of LexA: a conformational switch for regulation of self-cleavage

Crystal structure of a bacterial signal peptidase apoenzyme: implications for signal peptide binding and the Ser-Lys dyad mechanism

The crystal structure of the AAA domain of the ATP-dependent protease FtsH of Escherichia coli at 1.5 A resolution

Hexameric ring structure of the ATPase domain of the membrane-integrated metalloprotease FtsH from Thermus thermophilus HB8

Structure and reactivity of an asymmetric complex between HslV and I-domain deleted HslU, a prokaryotic homolog of the eukaryotic proteasome

The high-resolution X-ray crystal structure of the complex formed between subtilisin Carlsberg and eglin c, an elastase inhibitor from the leech Hirudo medicinalis. Structural analysis, subtilisin structure and interface geometry

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8140-8

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scholarly article

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3491550

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10.1074/JBC.M312243200

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9

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279

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Alexander Wlodawer

Zbigniew Dauter

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2004-02-27T00:00:00Z

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8967550

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14665623

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