Crystal structure of the dipeptide binding protein from Escherichia coli involved in active transport and chemotaxis.
about
Protein thiol modifications visualized in vivoLigand-induced conformational changes in a thermophilic ribose-binding proteinCompensating Stereochemical Changes Allow Murein Tripeptide to Be Accommodated in a Conventional Peptide-binding ProteinDelineation of the Pasteurellaceae-specific GbpA-family of glutathione-binding proteinsOn the binding mechanism of the peptide receptor of the oligopeptide transport system of Lactococcus lactisAn efficient computational method for calculating ligand binding affinitiesHigh-throughput screening of dipeptide utilization mediated by the ABC transporter DppBCDF and its substrate-binding proteins DppA1-A5 in Pseudomonas aeruginosaA Pyranose-2-Phosphate Motif Is Responsible for Both Antibiotic Import and Quorum-Sensing Regulation in Agrobacterium tumefaciensLigand Docking to Intermediate and Close-To-Bound Conformers Generated by an Elastic Network Model Based Algorithm for Highly Flexible ProteinsRepellent taxis in response to nickel ion requires neither Ni2+ transport nor the periplasmic NikA binding proteinDomains 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 housekeeping dipeptide permease is the Escherichia coli heme transporter and functions with two optional peptide binding proteins.Heme utilization by nontypeable Haemophilus influenzae is essential and dependent on Sap transporter functionStructural insights into the multispecific recognition of dipeptides of deep-sea gram-negative bacterium Pseudoalteromonas sp. strain SM9913.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.Kinetics and substrate specificity of membrane-reconstituted peptide transporter DtpT of Lactococcus lactisIsolation and characterization of mutants of the Bacillus subtilis oligopeptide permease with altered specificity of oligopeptide transport.Probing receptor-translocator interactions in the oligopeptide ABC transporter by fluorescence correlation spectroscopy.Modeling of the structure of the Haemophilus influenzae heme-binding protein suggests a mode of heme interaction.Ligand-dependent conformational plasticity of the periplasmic histidine-binding protein HisJ. Involvement in transport specificity.Identification of Ni-(L-His)₂ as a substrate for NikABCDE-dependent nickel uptake in Escherichia coli.Open Conformation of the Escherichia coli Periplasmic Murein Tripeptide Binding Protein, MppA, at High Resolution.Mutant Variants of the Substrate-Binding Protein DppA from Escherichia coli Enhance Growth on Nonstandard γ-Glutamyl Amide-Containing Peptides
P2860
Q24797314-C81B664E-5FFC-439C-90B7-A9D33B7C873DQ27652936-2D95733F-0366-4C36-8A57-2762689F04A4Q27670557-1796AC52-36FF-4FBD-B2EB-61F802AABBFAQ27675604-C3EF12EA-8776-4628-9A35-2B0958E81BC3Q28344489-292F1C93-17C5-4809-B933-65F078786217Q28482424-5A58F0B5-63C7-47CC-92DB-9C8C43EA934EQ28492467-A20EEEBE-D269-4F28-9843-8604BAA525CEQ28547025-FC81E71D-E189-4539-9F65-22FE1F9C3537Q28552181-F71AE168-76FC-4D77-A843-536F6DF1369DQ33826176-BC0B91DD-DA24-4527-AE5B-317A4C750AE4Q33963295-294BC4FA-D475-4289-AC28-1197874907E4Q35036520-B3A13E67-8D27-444D-88CD-0FA1FBACC92BQ35096143-7778AC86-240A-4C8F-8D2F-26ED175F9514Q35107287-85DB94F7-1EB1-401D-B4F4-8AE51840FBD9Q36639569-671BA8D9-976F-4C65-BAF1-900A056429B1Q37423462-18DFE7A9-61C8-45F7-9B03-48579C1F1612Q37471199-7FF11E44-F604-47F3-B160-B3223756044EQ39587399-7883A7F2-5255-4D18-AC0E-B774FDFE9AFEQ39981937-E3322B95-655D-4C29-B632-CB5A6F1F08B2Q42116100-7247010D-74F9-4455-B540-BC0A6522F100Q42646570-2FEB8ED1-7525-4781-B1E5-E84EF9BFB58BQ46687971-61F053D7-EF87-4155-8307-F921A0A7B510Q51553876-621819C7-25C4-4746-9A9F-0579A1C1773FQ55399024-285648FC-236A-4108-865C-39C146F8DC04Q56889992-D19C13F1-4189-4BE5-AB68-02AA9E3259B9
P2860
Crystal structure of the dipeptide binding protein from Escherichia coli involved in active transport and chemotaxis.
description
1995 nî lūn-bûn
@nan
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
1995年论文
@zh
1995年论文
@zh-cn
name
Crystal structure of the dipep ...... tive transport and chemotaxis.
@ast
Crystal structure of the dipep ...... tive transport and chemotaxis.
@en
type
label
Crystal structure of the dipep ...... tive transport and chemotaxis.
@ast
Crystal structure of the dipep ...... tive transport and chemotaxis.
@en
prefLabel
Crystal structure of the dipep ...... tive transport and chemotaxis.
@ast
Crystal structure of the dipep ...... tive transport and chemotaxis.
@en
P2860
P356
P1433
P1476
Crystal structure of the dipep ...... tive transport and chemotaxis.
@en
P2093
P2860
P304
P356
10.1002/PRO.5560041110
P577
1995-11-01T00:00:00Z