Crystal structure of the antibiotic albomycin in complex with the outer membrane transporter FhuA - Test2 - elhamkhani - TriplyDB

Crystal structure of the antibiotic albomycin in complex with the outer membrane transporter FhuA

Crystal structure of the antibiotic albomycin in complex with the outer membrane transporter FhuA

http://www.wikidata.org/entity/Q27624891

about

Siderophore-based iron acquisition and pathogen control X-ray crystallographic structures of the Escherichia coli periplasmic protein FhuD bound to hydroxamate-type siderophores and the antibiotic albomycin Dimerization of TonB is not essential for its binding to the outer membrane siderophore receptor FhuA of Escherichia coli The Staphylococcus aureus Siderophore Receptor HtsA Undergoes Localized Conformational Changes to Enclose Staphyloferrin A in an Arginine-rich Binding Pocket Structural basis for hijacking siderophore receptors by antimicrobial lasso peptides A hybrid ring-opening metathesis polymerization catalyst based on an engineered variant of the β-barrel protein FhuA.Does the lipid environment impact the open-state conductance of an engineered β-barrel protein nanopore?Engineering a rigid protein tunnel for biomolecular detection.Engineering of the E. coli outer membrane protein FhuA to overcome the hydrophobic mismatch in thick polymeric membranes Molecular dynamics simulations of the bacterial outer membrane protein FhuA: a comparative study of the ferrichrome-free and bound states FhuA barrel-cork hybrids are active transporters and receptors.Exchangeability of N termini in the ligand-gated porins of Escherichia coli.Outer membrane channels and active transporters for the uptake of antibiotics.Interactions among strategies associated with bacterial infection: pathogenicity, epidemicity, and antibiotic resistance TonB-dependent transporters: regulation, structure, and function.Ferredoxin containing bacteriocins suggest a novel mechanism of iron uptake in Pectobacterium spp Iron transport and signaling in Escherichia coli.Microbial iron acquisition: marine and terrestrial siderophores.Acquisition of siderophores in gram-negative bacteria.Global redesign of a native β-barrel scaffold.Inspection of the engineered FhuA ΔC/Δ4L protein nanopore by polymer exclusion.High resolution crystallographic studies of alpha-hemolysin-phospholipid complexes define heptamer-lipid head group interactions: implication for understanding protein-lipid interactions.Trihydroxamate siderophore-fluoroquinolone conjugates are selective sideromycin antibiotics that target Staphylococcus aureus.Biosynthetic tailoring of microcin E492m: post-translational modification affords an antibacterial siderophore-peptide conjugate.Is drug release necessary for antimicrobial activity of siderophore-drug conjugates? Syntheses and biological studies of the naturally occurring salmycin "Trojan Horse" antibiotics and synthetic desferridanoxamine-antibiotic conjugates FhuA (TonA), the career of a protein.Antibiotics from microbes: converging to kill.TonB or not TonB: is that the question?The role of bacterial membrane proteins in the internalization of microcin MccJ25 and MccB17.Fate of ferrisiderophores after import across bacterial outer membranes: different iron release strategies are observed in the cytoplasm or periplasm depending on the siderophore pathways.Siderophore-dependent iron uptake systems as gates for antibiotic Trojan horse strategies against Pseudomonas aeruginosa.Role of the Native Outer-Membrane Environment on the Transporter BtuB.Albomycin uptake via a ferric hydroxamate transport system of Streptococcus pneumoniae R6.Engineering of an E. coli outer membrane protein FhuA with increased channel diameter.The 'liaisons dangereuses' between iron and antibiotics.Contact Statistics Highlight Distinct Organizing Principles of Proteins and RNA Analysis of haptoglobin and hemoglobin-haptoglobin interactions with the Neisseria meningitidis TonB-dependent receptor HpuAB by flow cytometry.Loop deletions indicate regions important for FhuA transport and receptor functions in Escherichia coli The Pseudomonas aeruginosa PA14 ABC Transporter NppA1A2BCD Is Required for Uptake of Peptidyl Nucleoside Antibiotics.Sideromycins: tools and antibiotics

P2860

Q24681774-8FC33F41-9F60-4719-A2FA-2E5CAB3AADC2 Q27637443-0800202F-1FC6-4611-A5AA-5EA6D15BFE36 Q27642759-64E87FEE-0DC7-4C1D-BCF7-94A696EB3E46 Q27659711-AEC558C8-A9D7-40F7-9385-C37C218F3F4C Q27682973-FCC10EDE-6EDA-4385-B369-6F990BC6EDD6 Q30153526-38012609-E585-476D-AE02-0B37EDA6132C Q30155160-E38867D7-9B75-4589-A71A-DDDA845D3B49 Q30155319-20A1EE58-244D-44BF-9034-F3FAC48A7A5C Q30155616-85D1B7C7-A0D5-4F51-AB11-A920296F529E Q30164549-CC932D79-BE10-4717-A93E-6ADD6813777C Q30168191-F67D704B-E60F-4BD4-9FD9-40EAE491D48D Q30168335-F69C8B91-C9D4-47FD-8AF8-F8BCF0121AF7 Q31918231-81D198A9-5C48-4A2C-A0D0-2375C1B76773 Q34102811-8521E168-940D-44F2-AA95-92D67D7BB5CA Q34112189-F0E49AC3-69F2-4E2B-8FD7-2F6C1F15E44F Q34200327-F79CAB9F-BFCF-4071-B815-ECE6C27DFDC6 Q34922187-EEF26D67-FF67-44C2-AF7E-A057849E97F5 Q35004471-0458BB10-C00D-4BA9-A351-F23DAE8A0F8A Q35058516-984D3F85-B926-4DE8-9B4C-46CC46176C56 Q36328303-7561D4D2-FB8F-4163-BB04-51013366B65D Q36439499-ADA8BFCD-054B-4A4A-99EE-E2F7211D9A83 Q36519414-6FAD1143-B691-4FB1-8885-C2839BC765CF Q36787714-3A4EE38A-74B4-4954-8C03-FFDC0145E862 Q36848822-306DFF90-6AEA-4D9C-8321-9DC797B7F65B Q37394682-E2538C6A-15FD-4551-8A1B-D9E90CF647AA Q37426169-15D71D3F-FF53-4DF0-8DDE-F99666071FA6 Q37583238-F0600609-FCC0-40B2-B795-21231EB59BB2 Q37860145-137B9CC2-E078-4794-A62D-51C3DD5AE6B1 Q38062009-BEBB7FD0-D1E3-401F-AAF0-79F77767F574 Q38084924-0CF5296A-B89D-43DF-AC0D-A0A8BA79C72A Q38183671-96A5936A-50F8-43D7-AD0F-0E1AA229C5A7 Q38290733-4875A3F6-A35F-475F-9F45-5C7093E320EB Q38313213-DF474B3F-2C3B-4E3C-825D-28E1561689BC Q38366982-55C6DFDF-14C4-459F-9805-BB41D7B5D65D Q38761978-173D3028-2927-4567-8B84-F1FE3047262B Q39700715-7D01B35A-7EE7-48F1-BFEC-429A419879FA Q40763891-EDDFA5B4-066E-42E5-AEC8-461FBAFB711A Q40993353-6AEACD6A-EB24-4DB7-88E2-8F270BAE14E7 Q41007282-0168DB74-7D0F-4EB9-8F02-E5537D37C464 Q41440537-E8BB5C47-8239-4421-BCC0-29E4D03D52AA

P2860

Crystal structure of the antibiotic albomycin in complex with the outer membrane transporter FhuA

http://www.wikidata.org/entity/Q27624891

description

2000 nî lūn-bûn

@nan

2000 թուականի Մայիսին հրատարակուած գիտական յօդուած

@hyw

2000 թվականի մայիսին հրատարակված գիտական հոդված

@hy

2000年の論文

@ja

2000年論文

@yue

2000年論文

@zh-hant

2000年論文

@zh-hk

2000年論文

@zh-mo

2000年論文

@zh-tw

2000年论文

@wuu

name

Crystal structure of the antib ...... uter membrane transporter FhuA

@ast

Crystal structure of the antib ...... uter membrane transporter FhuA

@en

Crystal structure of the antib ...... uter membrane transporter FhuA

@nl

type

label

Crystal structure of the antib ...... uter membrane transporter FhuA

@ast

Crystal structure of the antib ...... uter membrane transporter FhuA

@en

Crystal structure of the antib ...... uter membrane transporter FhuA

@nl

prefLabel

Crystal structure of the antib ...... uter membrane transporter FhuA

@ast

Crystal structure of the antib ...... uter membrane transporter FhuA

@en

Crystal structure of the antib ...... uter membrane transporter FhuA

@nl

P1433

Q27624891-DBA85DC0-3995-4303-8311-A7287C473223

P1476

Q27624891-C2EB9201-2FFD-4C12-B94B-DAFEA89DA47A

P2093

Q27624891-20972C83-FCB0-4BA5-9168-AA0E00A0A200

Q27624891-61505334-0837-4637-ACBE-759189AF8B53

Q27624891-9811C3C2-5FCF-47F3-AB98-08FC8BE048F7

Q27624891-9F6F23C6-660C-4E2A-8118-75E9851C6AF3

Q27624891-AA25936C-7B64-40B4-B544-D2E75D872663

Q27624891-CD9BBCA4-ECC6-4024-83D2-CE3E37A60C9A

P2860

Q27624891-087AA7E8-E122-4496-BBDB-6A60EC83BEA0

Q27624891-0EA48529-78D5-4419-82F9-33F4286B0636

Q27624891-16F80A94-9993-412F-92C8-40D0FE5DE64C

Q27624891-2A112E3A-C313-492F-AC8A-95B2FF62EB1C

Q27624891-2E339BC0-0464-4418-8B8E-A61FEB195903

Q27624891-40BB9267-E638-47F5-ADAC-50A75684B65B

Q27624891-52126D1F-EA53-4D80-A95F-AB028AF0E23D

Q27624891-58761E24-719A-499B-9F18-D0A41C40D831

Q27624891-5B05A1A4-5C2F-48F8-A831-292207444C9B

Q27624891-5FA973DA-C588-47B3-920F-0B8FC3D97871

P304

Q27624891-9BF79E78-16E4-414F-97FE-B7ED526EEA01

P31

Q27624891-9531C1B0-D1D9-4AB4-9AC0-3CC31DDC23DF

P356

Q27624891-669853E6-EFA5-40EF-914D-B17EEDFEA3B1

P433

Q27624891-FEEB6936-6D06-4331-AC4A-5E427223962F

P478

Q27624891-84EF4B54-3655-4675-A9C5-65836265EDB2

P577

Q27624891-F227608C-BFB4-4B5F-BB0C-5FDADC5860AD

P5875

Q27624891-7D5EEADE-F17E-46C9-B2F5-C3343EF9043D

P698

Q27624891-16182433-B8F6-4F29-85C3-873BA55B75A4

P921

Q27624891-062A65E7-7298-4A1F-BC1E-9267C3F98F5B

Q27624891-6865A048-F514-443E-99A5-4661954FE486

P932

Q27624891-93874A79-ECDC-450B-96E4-C62CFE3E23CB

P356

P1433

Protein Science

P1476

Crystal structure of the antib ...... uter membrane transporter FhuA

@en

P2093

A D Ferguson

http://www.w3.org/2001/XMLSchema#string

H P Fiedler

http://www.w3.org/2001/XMLSchema#string

J W Coulton

http://www.w3.org/2001/XMLSchema#string

K Diederichs

http://www.w3.org/2001/XMLSchema#string

V Braun

http://www.w3.org/2001/XMLSchema#string

W Welte

http://www.w3.org/2001/XMLSchema#string

P2860

Improved methods for building protein models in electron density maps and the location of errors in these models

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

Siderophore-mediated iron transport: crystal structure of FhuA with bound lipopolysaccharide

Transmembrane signaling across the ligand-gated FhuA receptor: crystal structures of free and ferrichrome-bound states reveal allosteric changes

Genetic insertion and exposure of a reporter epitope in the ferrichrome-iron receptor of Escherichia coli K-12.

Genetic control of hydroxamate-mediated iron uptake in Escherichia coli.

Studies and syntheses of siderophores, microbial iron chelators, and analogs as potential drug delivery agents.

Siderophores: structure and function of microbial iron transport compounds.

Iron transport-mediated antibacterial activity of and development of resistance to hydroxamate and catechol siderophore-carbacephalosporin conjugates.

An internal affinity-tag for purification and crystallization of the siderophore receptor FhuA, integral outer membrane protein from Escherichia coli K-12.

P304

956-63

http://www.w3.org/2001/XMLSchema#string

P31

scholarly article

P356

10.1110/PS.9.5.956

http://www.w3.org/2001/XMLSchema#string

P433

5

http://www.w3.org/2001/XMLSchema#string

P478

9

http://www.w3.org/2001/XMLSchema#string

P577

2000-05-01T00:00:00Z

http://www.w3.org/2001/XMLSchema#dateTime

P5875

12467361

http://www.w3.org/2001/XMLSchema#string

P698

10850805

http://www.w3.org/2001/XMLSchema#string

P921

crystal structure

P932

2144648

http://www.w3.org/2001/XMLSchema#string