The structural basis of signal transduction for the response regulator PrrA from Mycobacterium tuberculosis
about
Prokaryotic 2-component systems and the OmpR/PhoB superfamilyStructure and dynamics of polymyxin-resistance-associated response regulator PmrA in complex with promoter DNAStructure of the response regulator VicR DNA-binding domainNMR structure of the pseudo-receiver domain of CikADomain Orientation in the Inactive Response Regulator Mycobacterium tuberculosis MtrA Provides a Barrier to Activation † , ‡Crystal Structures of the Receiver Domain of the Response Regulator PhoP from Escherichia coli in the Absence and Presence of the Phosphoryl Analog BeryllofluorideThe structure of a full-length response regulator from Mycobacterium tuberculosis in a stabilized three-dimensional domain-swapped, activated stateStructure of the DNA-Binding Domain of the Response Regulator PhoP from Mycobacterium tuberculosis † , ‡Regulation of Response Regulator Autophosphorylation through Interdomain ContactsStructure of the Response Regulator PhoP from Mycobacterium tuberculosis Reveals a Dimer through the Receiver DomainThe dimeric form of the unphosphorylated response regulator BaeRSolution structure and tandem DNA recognition of the C-terminal effector domain of PmrA from Klebsiella pneumoniaeAn asymmetric heterodomain interface stabilizes a response regulator–DNA complexAtypical Response Regulator ChxR from Chlamydia trachomatis Is Structurally Poised for DNA BindingAtypical OmpR/PhoB Subfamily Response Regulator GlnR of Actinomycetes Functions as a Homodimer, Stabilized by the Unphosphorylated Conserved Asp-focused Charge InteractionsStructural dynamics of the two-component response regulator RstA in recognition of promoter DNA elementStructure of the DNA-binding domain of the response regulator SaeR from Staphylococcus aureusPhosphorylation of PhoP protein plays direct regulatory role in lipid biosynthesis of Mycobacterium tuberculosisX-ray solution scattering (SAXS) combined with crystallography and computation: defining accurate macromolecular structures, conformations and assemblies in solutionDistinct single amino acid replacements in the control of virulence regulator protein differentially impact streptococcal pathogenesisAdaptation to environmental stimuli within the host: two-component signal transduction systems of Mycobacterium tuberculosis.The prrAB two-component system is essential for Mycobacterium tuberculosis viability and is induced under nitrogen-limiting conditionsConformational Dynamics of Response Regulator RegX3 from Mycobacterium tuberculosis.Structure of the Response Regulator NsrR from Streptococcus agalactiae, Which Is Involved in Lantibiotic Resistance.Bacterial response regulators: versatile regulatory strategies from common domains.Structure and flexibility within proteins as identified through small angle X-ray scatteringBiological insights from structures of two-component proteins.To ∼P or Not to ∼P? Non-canonical activation by two-component response regulators.Molecular strategies for phosphorylation-mediated regulation of response regulator activity.Homology modeling, molecular dynamics and QM/MM study of the regulatory protein PhoP from Corynebacterium pseudotuberculosis.Mycobacterium tuberculosis PhoP recognizes two adjacent direct-repeat sequences to form head-to-head dimers.Unique N-terminal arm of Mycobacterium tuberculosis PhoP protein plays an unusual role in its regulatory function.Domain structure of virulence-associated response regulator PhoP of Mycobacterium tuberculosis: role of the linker region in regulator-promoter interaction(s).Structural mechanism of signal transduction between the RNA-binding domain and the phosphotransferase system regulation domain of the LicT antiterminator.Evolutionary analysis and lateral gene transfer of two-component regulatory systems associated with heavy-metal tolerance in bacteria.Dual phosphorylation in response regulator protein PrrA is crucial for intracellular survival of mycobacteria consequent upon transcriptional activation.A new and unexpected domain-domain interaction in the AraC protein.
P2860
Q26783533-13328AA0-E80F-4DD4-82CD-B90B38D58D07Q27318559-4D7A4301-AA2D-45B6-B764-46D931A49AEAQ27643628-7CF0994D-6ADA-484F-98D4-2011ADF6A444Q27643902-5B5808E5-C343-4766-94C0-4761C67C773AQ27644822-8D6B639A-D3D7-44B1-9A13-9CCDCB2511DBQ27645204-6EF23F5F-25D6-4627-9DFF-87E0CA6B411CQ27648812-3ECB31B9-31F9-4443-A80A-4C3325E79E15Q27649175-CBA1A11D-7302-4569-A8E5-96B1BEEAAA52Q27664032-A55B5EE0-C422-437B-A259-F5BCD85B33C1Q27668141-E3040AB9-24A9-4B0C-A9B8-3999012F8312Q27679136-5AA8C249-491E-4ECF-9CA8-B31F9E96B909Q27681103-E05EA34D-0D96-4DE7-A186-2287C62D7789Q27681718-3C22AEEF-A0AD-44AB-9363-4C3AACB3B16DQ27682297-915CF5BE-94E8-4E26-9D3D-70F9F410F5DEQ27683358-BB9CCE63-E13C-4044-B55C-015B4707C3FCQ27684524-BFEE7E9B-82DD-480C-B289-76ED1DA4E577Q27701754-3EED2586-181C-4E12-BE43-FF9CD29C54E0Q28487131-410EA061-3317-4ACC-B485-4E80B0C10F54Q29619405-AC3D19CB-E9AB-4990-8754-B865174415DCQ30408643-028F226A-737B-423F-9B2B-11AAF617A569Q35598334-B6B62562-3220-423E-8503-A69A3E548502Q35668167-61A98B95-3A7B-4401-8581-AB54EA5C0AA1Q35705768-592D9A09-8630-40B9-A7C1-A3FF59D905DDQ35940689-10A050D5-024F-47E1-B8AB-17FCE6092577Q36791337-214AEF76-3689-4EF4-AC2B-B17A412899E7Q37172360-4D347646-0401-4278-884A-14D71332782CQ37539921-453F7A19-D9DD-494F-AF13-8F9E2CE5B8C6Q37568709-4174E36D-CE9C-44DD-98FD-0B2089EF0478Q37676555-13441BA5-BA02-47D3-A37C-83623F720806Q39736119-7BBE523D-E1AA-47E5-8668-9A158A326ADDQ41773031-999687CC-87B6-45CC-8F7B-C9F5337E53F7Q41880717-2FF13E28-AD4A-47F9-A24C-AC2020C9E0E7Q41969863-C2320581-4B56-4F28-A974-00D15C49E7CCQ43154755-3021FCFA-E955-48F2-B1BA-99862AF7F168Q43634018-80FEDCF1-6107-4DC1-8163-795651764D08Q47442954-1ABBDF4D-9C09-427D-AF0C-D83ABD6E67A0Q54341267-5EF0F3F9-737F-4579-943E-A3A5BE81B262
P2860
The structural basis of signal transduction for the response regulator PrrA from Mycobacterium tuberculosis
description
2006 թուականի Ապրիլին հրատարակուած գիտական յօդուած
@hyw
2006 թվականի ապրիլին հրատարակված գիտական հոդված
@hy
article publié dans la revue scientifique Journal of Biological Chemistry
@fr
artículu científicu espublizáu en 2006
@ast
im April 2006 veröffentlichter wissenschaftlicher Artikel
@de
scientific journal article
@en
vedecký článok (publikovaný 2006/04/07)
@sk
vědecký článek publikovaný v roce 2006
@cs
wetenschappelijk artikel (gepubliceerd op 2006/04/07)
@nl
наукова стаття, опублікована у квітні 2006
@uk
name
The structural basis of signal ...... rom Mycobacterium tuberculosis
@ast
The structural basis of signal ...... rom Mycobacterium tuberculosis
@en
The structural basis of signal ...... rom Mycobacterium tuberculosis
@nl
type
label
The structural basis of signal ...... rom Mycobacterium tuberculosis
@ast
The structural basis of signal ...... rom Mycobacterium tuberculosis
@en
The structural basis of signal ...... rom Mycobacterium tuberculosis
@nl
prefLabel
The structural basis of signal ...... rom Mycobacterium tuberculosis
@ast
The structural basis of signal ...... rom Mycobacterium tuberculosis
@en
The structural basis of signal ...... rom Mycobacterium tuberculosis
@nl
P2093
P2860
P356
P1476
The structural basis of signal ...... rom Mycobacterium tuberculosis
@en
P2093
Elzbieta Nowak
Paul A Tucker
Peter Konarev
P2860
P304
P356
10.1074/JBC.M512004200
P407
P577
2006-01-23T00:00:00Z