Crystal structure of a bacterial signal peptidase apoenzyme: implications for signal peptide binding and the Ser-Lys dyad mechanism
about
Structure of malonamidase E2 reveals a novel Ser-cisSer-Lys catalytic triad in a new serine hydrolase fold that is prevalent in nature"Splicing up" drug discovery. Cell-based expression and screening of genetically-encoded libraries of backbone-cyclized polypeptidesCrystal structure of microbial transglutaminase from Streptoverticillium mobaraenseThe catalytic domain of Escherichia coli Lon protease has a unique fold and a Ser-Lys dyad in the active siteCrystal 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 activityCrystal Structure of a Viral Protease Intramolecular Acyl-enzyme Complex: INSIGHTS INTO cis-CLEAVAGE AT THE VP4/VP3 JUNCTION OF TELLINA BIRNAVIRUSSynthesis and Characterization of the Arylomycin Lipoglycopeptide Antibiotics and the Crystallographic Analysis of Their Complex with Signal PeptidaseCrystal Structures of Yellowtail Ascites Virus VP4 Protease: TRAPPING AN INTERNAL CLEAVAGE SITE TRANS ACYL-ENZYME COMPLEX IN A NATIVE SER/LYS DYAD ACTIVE SITEUnconventional serine proteases: variations on the catalytic Ser/His/Asp triad configurationProtein secretion and outer membrane assembly in AlphaproteobacteriaSolution NMR of signal peptidase, a membrane protein.Expressed protein ligation: a resourceful tool to study protein structure and function.Peptide binding to a bacterial signal peptidase visualized by peptide tethering and carrier-driven crystallizationThe active site of a lon protease from Methanococcus jannaschii distinctly differs from the canonical catalytic Dyad of Lon proteases.Altered -3 substrate specificity of Escherichia coli signal peptidase 1 mutants as revealed by screening a combinatorial peptide library.Modeling Escherichia coli signal peptidase complex with bound substrate: determinants in the mature peptide influencing signal peptide cleavageFlanking signal and mature peptide residues influence signal peptide cleavage.Endopeptidase activity characterization of E. coli-derived infectious bursal disease virus protein 4 tubules.Initial efforts toward the optimization of arylomycins for antibiotic activity.Molecular analysis of Phr peptide processing in Bacillus subtilisCASTp: Computed Atlas of Surface Topography of proteins.Molecular engineering of secretory machinery components for high-level secretion of proteins in Bacillus species.Structural studies of a signal peptide in complex with signal peptidase I cytoplasmic domain: the stabilizing effect of membrane-mimetics on the acquired foldBiological activities of natural and engineered cyclotides, a novel molecular scaffold for peptide-based therapeutics.Cyclotides, a novel ultrastable polypeptide scaffold for drug discoveryWhat Makes a Bacterial Species Pathogenic?:Comparative Genomic Analysis of the Genus LeptospiraExpression, 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 virusSlicing a protease: structural features of the ATP-dependent Lon proteases gleaned from investigations of isolated domains.Interactions that drive Sec-dependent bacterial protein transport.A small subset of signal peptidase residues are perturbed by signal peptide binding.Purification and characterization of the repressor of the shiga toxin-encoding bacteriophage 933W: DNA binding, gene regulation, and autocleavage.Fluorescence spectroscopy of soluble E. coli SPase I Δ2-75 reveals conformational changes in response to ligand binding.S-layer glycoproteins and flagellins: reporters of archaeal posttranslational modifications.Signal peptidase I: cleaving the way to mature proteins.Bacterial type I signal peptidases as antibiotic targets.Structure of the Cyanuric Acid Hydrolase TrzD Reveals Product Exit Channel.Site-directed mutagenesis analysis of amino acids critical for activity of the type I signal peptidase of the archaeon Methanococcus voltae.Genetic complementation in yeast reveals functional similarities between the catalytic subunits of mammalian signal peptidase complex.
P2860
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P2860
Crystal structure of a bacterial signal peptidase apoenzyme: implications for signal peptide binding and the Ser-Lys dyad mechanism
description
2002 nî lūn-bûn
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2002 թուականի Մարտին հրատարակուած գիտական յօդուած
@hyw
2002 թվականի մարտին հրատարակված գիտական հոդված
@hy
2002年の論文
@ja
2002年論文
@yue
2002年論文
@zh-hant
2002年論文
@zh-hk
2002年論文
@zh-mo
2002年論文
@zh-tw
2002年论文
@wuu
name
Crystal structure of a bacteri ...... and the Ser-Lys dyad mechanism
@ast
Crystal structure of a bacteri ...... and the Ser-Lys dyad mechanism
@en
Crystal structure of a bacteri ...... and the Ser-Lys dyad mechanism
@nl
type
label
Crystal structure of a bacteri ...... and the Ser-Lys dyad mechanism
@ast
Crystal structure of a bacteri ...... and the Ser-Lys dyad mechanism
@en
Crystal structure of a bacteri ...... and the Ser-Lys dyad mechanism
@nl
prefLabel
Crystal structure of a bacteri ...... and the Ser-Lys dyad mechanism
@ast
Crystal structure of a bacteri ...... and the Ser-Lys dyad mechanism
@en
Crystal structure of a bacteri ...... and the Ser-Lys dyad mechanism
@nl
P2860
P356
P1476
Crystal structure of a bacteri ...... and the Ser-Lys dyad mechanism
@en
P2093
Natalie C J Strynadka
Ross E Dalbey
P2860
P304
P356
10.1074/JBC.M110983200
P407
P50
P577
2002-03-15T00:00:00Z