Structure of FitAB from Neisseria gonorrhoeae bound to DNA reveals a tetramer of toxin-antitoxin heterodimers containing pin domains and ribbon-helix-helix motifs
about
Structure and proposed activity of a member of the VapBC family of toxin-antitoxin systems. VapBC-5 from Mycobacterium tuberculosisKeeping the Wolves at Bay: Antitoxins of Prokaryotic Type II Toxin-Antitoxin SystemsEffect of rickettsial toxin VapC on its eukaryotic hostMolecular and structural characterization of the PezAT chromosomal toxin-antitoxin system of the human pathogen Streptococcus pneumoniaeThe solution structure of ParD, the antidote of the ParDE toxin-antitoxin module, provides the structural basis for DNA and toxin bindingCrystal structure of PAE0151 from Pyrobaculum aerophilum, a PIN-domain (VapC) protein from a toxin-antitoxin operonStructural Basis of the Transcriptional Regulation of the Proline Utilization Regulon by Multifunctional PutAStructure, Function, and Targets of the Transcriptional Regulator SvtR from the Hyperthermophilic Archaeal Virus SIRV1The Staphylococcus aureus pSK41 plasmid-encoded ArtA protein is a master regulator of plasmid transmission genes and contains a RHH motif used in alternate DNA-binding modesSolution Structure and Membrane Binding of the Toxin Fst of the par Addiction ModuleStructure of the Escherichia coli Antitoxin MqsA (YgiT/b3021) Bound to Its Gene Promoter Reveals Extensive Domain Rearrangements and the Specificity of Transcriptional RegulationCrystal structure and centromere binding of the plasmid segregation protein ParB from pCXC100The Structure and Interactions of SpoIISA and SpoIISB, a Toxin-Antitoxin System in Bacillus subtilisThe crystal structure of the Rv0301-Rv0300 VapBC-3 toxin-antitoxin complex fromM. tuberculosisreveals a Mg2+ion in the active site and a putative RNA-binding siteStructure and Function of AvtR, a Novel Transcriptional Regulator from a Hyperthermophilic Archaeal LipothrixvirusCrystal Structure of the VapBC Toxin–Antitoxin Complex from Shigella flexneri Reveals a Hetero-Octameric DNA-Binding AssemblyCrystal structure of the DNA-bound VapBC2 antitoxin/toxin pair from Rickettsia felisStructural Studies of E73 from a Hyperthermophilic Archaeal Virus Identify the “RH3” Domain, an Elaborated Ribbon–Helix–Helix Motif Involved in DNA RecognitionThe Transcription Factor AmrZ Utilizes Multiple DNA Binding Modes to Recognize Activator and Repressor Sequences of Pseudomonas aeruginosa Virulence GenesStructural Basis of mRNA Recognition and Cleavage by Toxin MazF and Its Regulation by Antitoxin MazE in Bacillus subtilisStructure of the Proteus vulgaris HigB-(HigA)2-HigB Toxin-Antitoxin ComplexCrystal structure of toxin HP0892 fromHelicobacter pyloriwith two Zn(II) at 1.8 Å resolutionMechanisms of Toxin Inhibition and Transcriptional Repression by Escherichia coli DinJ-YafQStructural analysis of the active site architecture of the VapC toxin from Shigella flexneriNob1 binds the single-stranded cleavage site D at the 3'-end of 18S rRNA with its PIN domain.Structure, Biology, and Therapeutic Application of Toxin-Antitoxin Systems in Pathogenic BacteriaNoncognate Mycobacterium tuberculosis toxin-antitoxins can physically and functionally interactAnalysis of non-typeable Haemophilous influenzae VapC1 mutations reveals structural features required for toxicity and flexibility in the active siteToxin inhibition in C. crescentus VapBC1 is mediated by a flexible pseudo-palindromic protein motif and modulated by DNA binding.The relBE2Spn toxin-antitoxin system of Streptococcus pneumoniae: role in antibiotic tolerance and functional conservation in clinical isolates.Independent evolution of the core and accessory gene sets in the genus Neisseria: insights gained from the genome of Neisseria lactamica isolate 020-06.Comprehensive classification of the PIN domain-like superfamilyVapC from the leptospiral VapBC toxin-antitoxin module displays ribonuclease activity on the initiator tRNA.VapC toxins from Mycobacterium tuberculosis are ribonucleases that differentially inhibit growth and are neutralized by cognate VapB antitoxins.The PIN-domain ribonucleases and the prokaryotic VapBC toxin-antitoxin array.Plasmid addiction systems: perspectives and applications in biotechnology.Enteric virulence associated protein VapC inhibits translation by cleavage of initiator tRNADetermination of ribonuclease sequence-specificity using Pentaprobes and mass spectrometry.A VapBC toxin-antitoxin module is a posttranscriptional regulator of metabolic flux in mycobacteria.Regulation of the Escherichia coli HipBA toxin-antitoxin system by proteolysis
P2860
Q24656034-F3462D25-E9F4-4F99-B193-901782FB1761Q26751512-06132F5D-C101-4F03-AB0B-9398CF6CB90EQ27315904-93BB1AEC-768F-44B2-A983-CE5B9C019709Q27644721-C7BA6D0E-60E2-4286-BE3B-D0A742E01A9DQ27646891-53B107BC-7B21-46C0-9DB5-5CD93C84244EQ27650276-3A6AE6B6-2BB6-4075-B3F2-4A799986C0E9Q27650991-E8B2C098-2309-430F-B486-92190B5059FCQ27656008-6FF8F329-C5D4-4D45-A927-5575E074BA21Q27657447-D2A3AC74-8D60-4C07-87D5-0B2FE3C4C7F2Q27663801-94C24C85-CCED-4CF2-A927-AA5EEADD8233Q27665770-4A41C387-1E0A-4BE3-A837-245E502D782AQ27666129-FBBB0E3C-793D-4AF4-A9F2-0196942484BFQ27666312-A97D5543-689C-4960-8ACA-863928B341C0Q27673611-B9624E17-6DC5-438D-A143-6166DF60D967Q27674412-549FA28D-9530-4ED2-8663-F619D54CCC68Q27675281-13CEEF21-07B7-4756-AB69-0127D98E515BQ27675975-B519010E-6DE9-4F45-92F4-BBC5A59B1B79Q27678006-A9E4EFDE-9672-4C17-9799-2A8BCA1E065BQ27678592-207C656E-11B9-4ED4-AF70-0BA868FF1EE2Q27680238-70BE6158-32B1-4935-8396-BD94EC85D12FQ27680659-4B3E3AD7-0937-47C6-8019-14B59AD4A3C9Q27682631-E75ACAC5-9D1E-4187-AD2D-D25DE76B981DQ27684081-1F3C7C99-9236-45BF-AF5C-FEA11894717CQ27703785-ABAE2380-A4C0-475A-8826-40D611D16F19Q27938030-4E6CDB0B-0842-4AA0-B43F-8DFEF1AB5B85Q28066978-315450EA-6B48-44EA-8CD8-45A6D1E39997Q28487395-E74ABD65-452C-4316-9EA9-3BAB24FBB2C7Q28544904-FA3E67E2-D1DA-4B42-9EC6-E3EE6C7B7B25Q33558196-6567BC41-9841-4ED9-B30C-603530CE3DEEQ33619338-E1F538BD-B6F7-4D4F-9C6F-13D0BDD72237Q33752108-C8E43083-D290-441B-BA3C-7F518EADB4E9Q33878209-7180119C-775E-49E6-ADBC-FB749FD41BD9Q33927697-6FB9B58D-063A-4C37-9289-BB7295084D37Q33955336-FDB0725C-E4E9-4643-A64A-9C9886BFDDBFQ34147063-84BF4541-9A08-440B-93B9-0CF8AC094F6AQ34160193-6AEA01E5-DBB3-4D9B-8215-57701D9FA342Q34179250-76DA92DA-B275-4D1D-9D82-0F68E2070266Q34249245-DF82373A-B93F-43E7-A376-6988AF0E9D6FQ34256988-00E8B35C-B955-4DA8-9E57-237D8495705BQ34312265-146EF8DD-4B93-4F43-9FF0-5763CAFA3A63
P2860
Structure of FitAB from Neisseria gonorrhoeae bound to DNA reveals a tetramer of toxin-antitoxin heterodimers containing pin domains and ribbon-helix-helix motifs
description
2006 թուականի Դեկտեմբերին հրատարակուած գիտական յօդուած
@hyw
2006 թվականի դեկտեմբերին հրատարակված գիտական հոդված
@hy
article publié dans la revue scientifique Journal of Biological Chemistry
@fr
artículu científicu espublizáu en 2006
@ast
im Dezember 2006 veröffentlichter wissenschaftlicher Artikel
@de
scientific journal article
@en
vedecký článok (publikovaný 2006/12/08)
@sk
vědecký článek publikovaný v roce 2006
@cs
wetenschappelijk artikel (gepubliceerd op 2006/12/08)
@nl
наукова стаття, опублікована в грудні 2006
@uk
name
Structure of FitAB from Neisse ...... and ribbon-helix-helix motifs
@ast
Structure of FitAB from Neisse ...... and ribbon-helix-helix motifs
@en
Structure of FitAB from Neisse ...... and ribbon-helix-helix motifs
@nl
type
label
Structure of FitAB from Neisse ...... and ribbon-helix-helix motifs
@ast
Structure of FitAB from Neisse ...... and ribbon-helix-helix motifs
@en
Structure of FitAB from Neisse ...... and ribbon-helix-helix motifs
@nl
prefLabel
Structure of FitAB from Neisse ...... and ribbon-helix-helix motifs
@ast
Structure of FitAB from Neisse ...... and ribbon-helix-helix motifs
@en
Structure of FitAB from Neisse ...... and ribbon-helix-helix motifs
@nl
P2093
P2860
P3181
P356
P1476
Structure of FitAB from Neisse ...... and ribbon-helix-helix motifs
@en
P2093
J Scott Wilbur
Kirsten Mattison
Richard G Brennan
P2860
P304
37942-37951
P3181
P356
10.1074/JBC.M605198200
P407
P50
P577
2006-09-18T00:00:00Z