2 A resolution structure of DppA, a periplasmic dipeptide transport/chemosensory receptor
about
Molecular insights into proton coupled peptide transport in the PTR family of oligopeptide transportersCrystal structures of the liganded and unliganded nickel-binding protein NikA from Escherichia coliLigand-induced conformational changes in a thermophilic ribose-binding proteinThe structural basis for peptide selection by the transport receptor OppAGlutathione import in Haemophilus influenzae Rd is primed by the periplasmic heme-binding protein HbpAImportance of a Hydrophobic Pocket for Peptide Binding in Lactococcal OppACompensating Stereochemical Changes Allow Murein Tripeptide to Be Accommodated in a Conventional Peptide-binding ProteinStructure and Mode of Peptide Binding of Pheromone Receptor PrgZCrystal structure and mutational analysis of the Escherichia coli putrescine receptor. Structural basis for substrate specificityOn the binding mechanism of the peptide receptor of the oligopeptide transport system of Lactococcus lactisAn efficient computational method for calculating ligand binding affinitiesAn oligopeptide transporter of Mycobacterium tuberculosis regulates cytokine release and apoptosis of infected macrophagesHigh-throughput screening of dipeptide utilization mediated by the ABC transporter DppBCDF and its substrate-binding proteins DppA1-A5 in Pseudomonas aeruginosaLigand Docking to Intermediate and Close-To-Bound Conformers Generated by an Elastic Network Model Based Algorithm for Highly Flexible ProteinsStructural trees for protein superfamilies.Polyamine transport in bacteria and yeast.Domains III and I-2{alpha}, at the entrance of the binding cleft, play an important role in cold adaptation of the periplasmic dipeptide-binding protein (DppA) from the deep-sea psychrophilic bacterium Pseudoalteromonas sp. strain SM9913The change of protein intradomain mobility on ligand binding: is it a commonly observed phenomenon?Structural insights into the multispecific recognition of dipeptides of deep-sea gram-negative bacterium Pseudoalteromonas sp. strain SM9913.Conversion of a maltose receptor into a zinc biosensor by computational design.Intestinal peptidases form functional complexes with the neutral amino acid transporter B(0)AT1.Cadmium-induced crystallization of proteins: II. Crystallization of the Salmonella typhimurium histidine-binding protein in complex with L-histidine, L-arginine, or L-lysineABC transporter architecture and regulatory roles of accessory domains.The periplasmic disulfide oxidoreductase DsbA contributes to Haemophilus influenzae pathogenesis.Construction of a fluorescent biosensor family.Evaluation of the relative stability of liganded versus ligand-free protein conformations using Simplicial Neighborhood Analysis of Protein Packing (SNAPP) method.The membrane-associated lipoprotein-9 GmpC from Staphylococcus aureus binds the dipeptide GlyMet via side chain interactions.Specificity mutants of the binding protein of the oligopeptide transport system of Lactococcus lactis.Isolation of a periplasmic molecular chaperone-like protein of Rhodobacter sphaeroides f. sp. denitrificans that is homologous to the dipeptide transport protein DppA of Escherichia coli.Atomic structure and specificity of bacterial periplasmic receptors for active transport and chemotaxis: variation of common themes.Probing receptor-translocator interactions in the oligopeptide ABC transporter by fluorescence correlation spectroscopy.Dominant role of local dipolar interactions in phosphate binding to a receptor cleft with an electronegative charge surface: equilibrium, kinetic, and crystallographic studies.Berkeley Screen: a set of 96 solutions for general macromolecular crystallization.Crystal structure of a putative oligopeptide-binding periplasmic protein from a hyperthermophile.Inter-domain electron transfer in cellobiose dehydrogenase: modulation by pH and divalent cations.In vivo substrate specificity of periplasmic disulfide oxidoreductases.Ligand-dependent conformational plasticity of the periplasmic histidine-binding protein HisJ. Involvement in transport specificity.Open Conformation of the Escherichia coli Periplasmic Murein Tripeptide Binding Protein, MppA, at High Resolution.
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P2860
2 A resolution structure of DppA, a periplasmic dipeptide transport/chemosensory receptor
description
1995 nî lūn-bûn
@nan
1995 թուականի Դեկտեմբերին հրատարակուած գիտական յօդուած
@hyw
1995 թվականի դեկտեմբերին հրատարակված գիտական հոդված
@hy
1995年の論文
@ja
1995年論文
@yue
1995年論文
@zh-hant
1995年論文
@zh-hk
1995年論文
@zh-mo
1995年論文
@zh-tw
1995年论文
@wuu
name
2 A resolution structure of DppA, a periplasmic dipeptide transport/chemosensory receptor
@ast
2 A resolution structure of DppA, a periplasmic dipeptide transport/chemosensory receptor
@en
2 A resolution structure of DppA, a periplasmic dipeptide transport/chemosensory receptor
@nl
type
label
2 A resolution structure of DppA, a periplasmic dipeptide transport/chemosensory receptor
@ast
2 A resolution structure of DppA, a periplasmic dipeptide transport/chemosensory receptor
@en
2 A resolution structure of DppA, a periplasmic dipeptide transport/chemosensory receptor
@nl
prefLabel
2 A resolution structure of DppA, a periplasmic dipeptide transport/chemosensory receptor
@ast
2 A resolution structure of DppA, a periplasmic dipeptide transport/chemosensory receptor
@en
2 A resolution structure of DppA, a periplasmic dipeptide transport/chemosensory receptor
@nl
P2093
P3181
P356
P1433
P1476
2 A resolution structure of DppA, a periplasmic dipeptide transport/chemosensory receptor
@en
P2093
A V Nickitenko
F A Quiocho
S Trakhanov
P304
P3181
P356
10.1021/BI00051A006
P407
P577
1995-12-26T00:00:00Z