Membrane alignment of the pore-forming component TatA(d) of the twin-arginine translocase from Bacillus subtilis resolved by solid-state NMR spectroscopy.
about
The magic of bicelles lights up membrane protein structureSubstrate-dependent assembly of the Tat translocase as observed in live Escherichia coli cellsStructural model for the protein-translocating element of the twin-arginine transport systemConserved Signal Peptide Recognition Systems across the Prokaryotic DomainsStructural Basis for TatA Oligomerization: An NMR Study of Escherichia coli TatA Dimeric StructureUV-CD12: synchrotron radiation circular dichroism beamline at ANKA.Secretome of obligate intracellular Rickettsia.Towards understanding the Tat translocation mechanism through structural and biophysical studies of the amphipathic region of TatA from Escherichia coli.Hydrophobic Mismatch Drives the Interaction of E5 with the Transmembrane Segment of PDGF Receptor.The chloroplast twin arginine transport (Tat) component, Tha4, undergoes conformational changes leading to Tat protein transport.When detergent meets bilayer: birth and coming of age of lipid bicelles.Investigating the interaction between peptides of the amphipathic helix of Hcf106 and the phospholipid bilayer by solid-state NMR spectroscopy.Structure determination of membrane proteins in five easy piecesTwin-arginine-dependent translocation of folded proteins.The twin-arginine translocation (Tat) protein export pathway.Mechanistic Aspects of Folded Protein Transport by the Twin Arginine Translocase (Tat).Ultrastructural characterisation of Bacillus subtilis TatA complexes suggests they are too small to form homooligomeric translocation pores.Twin-Arginine Protein Translocation.Salt sensitivity of minimal twin arginine translocases.Early contacts between substrate proteins and TatA translocase component in twin-arginine translocation.3D hydrophobic moment vectors as a tool to characterize the surface polarity of amphiphilic peptides.In vivo experiments do not support the charge zipper model for Tat translocase assemblyStructure of TatA paralog, TatE, suggests a structurally homogeneous form of Tat protein translocase that transports folded proteins of differing diameter.Transmembrane insertion of twin-arginine signal peptides is driven by TatC and regulated by TatB.Escherichia coli TatA and TatB proteins have N-out, C-in topology in intact cells.The Tat system for membrane translocation of folded proteins recruits the membrane-stabilizing Psp machinery in Escherichia coli.Direct interaction between a precursor mature domain and transport component Tha4 during twin arginine transport of chloroplasts.Comparative analysis of the orientation of transmembrane peptides using solid-state (2)H- and (15)N-NMR: mobility matters.Structural features of the TatC membrane protein that determine docking and insertion of a twin-arginine signal peptide.Unanticipated functional diversity among the TatA-type components of the Tat protein translocase.Magnetically Alignable Bicelles with Unprecedented Stability Using Tunable Surfactants Derived from Cholic Acid.The TatA component of the twin-arginine translocation system locally weakens the cytoplasmic membrane of Escherichia coli upon protein substrate binding.Homo- and heteromeric interaction strengths of the synergistic antimicrobial peptides PGLa and magainin 2 in membranes
P2860
Q26991483-60054DC3-7F09-4D21-943E-BC55790B6ADEQ27311011-C282BE56-73A3-4F30-9F98-4866B3AA49B8Q27676737-BC7A8F4C-7E23-4EC1-BB84-25C6228C62A6Q27676944-2790802B-A54B-4C23-82D4-08A8D8C4A1BEQ27684932-9E4DE1DA-DA9D-467A-BE48-BEBC006D84D0Q30411317-88B3D822-5682-4039-AA69-C8936235BCA7Q35132653-0A742221-A8DD-4106-B54F-665D415BA5B2Q35790869-B58F77EE-60C8-47EE-B208-A6357F1EA90EQ35990329-BEDA41D8-2B46-4432-8A02-F4D800F7B7EEQ36298510-9725BD0E-9DC8-4170-B974-13CA471453DDQ37090616-71F2D441-C813-4912-A1ED-AC2CF6D06A81Q37394596-9047EECD-2D2B-4193-A9BF-517DEDD7CDDDQ37941436-AABCA138-8D39-4862-A853-0096F66B632AQ37993035-89D69E3C-3835-4EDB-B935-B2A10B4DCF72Q38017546-4EBC7CD4-908B-49E7-ADEA-DEBAFB94F622Q38480343-7D91F6CF-EE3D-4AB0-8D03-40ABE8B47DC2Q38787074-9A3DABDA-8210-4B08-9BB0-BA87C434BDF5Q38819418-3674B232-75D3-4C24-9431-ED0BC03F370BQ39935919-6FA3F4C9-4730-464D-B629-3BAF477E8791Q39936045-889783CE-A420-47EB-B551-DCBBC00EAF90Q40537362-E53D1B85-3CFA-4F62-A840-7BE378637EEEQ41720409-6368AB04-F543-43A8-8AA6-6A905BB56AEBQ41873284-5BF9BD3C-BCE3-4525-855A-DC71391AE677Q41913286-8A2E5847-186E-47E4-AE7E-E833C9EFAA06Q42141474-9266A0F0-7C75-4532-94CD-E8AF37C2C63EQ42322225-0876829A-C296-4484-92DA-3BB9486E53A7Q43458977-A9B632BF-4A79-4A45-881B-1DCE3DCC7E82Q46769517-F76DB8E8-EDFA-466A-BF55-A171A2C7C198Q47581014-69C9398B-D7C3-4141-8C99-4D3A1CCB4F7EQ48044430-07250B4F-A546-4F85-8024-E01CE17EAF40Q51187915-4AB012E1-48F8-4AC0-AE22-8B91BCFE731FQ54208079-2DE03FC5-E7ED-4525-BFB5-20B9854E0E34Q57528296-C970E58A-1460-4192-9AE2-DCA8B6388B75
P2860
Membrane alignment of the pore-forming component TatA(d) of the twin-arginine translocase from Bacillus subtilis resolved by solid-state NMR spectroscopy.
description
2010 nî lūn-bûn
@nan
2010年の論文
@ja
2010年論文
@yue
2010年論文
@zh-hant
2010年論文
@zh-hk
2010年論文
@zh-mo
2010年論文
@zh-tw
2010年论文
@wuu
2010年论文
@zh
2010年论文
@zh-cn
name
Membrane alignment of the pore-forming component TatA
@nl
Membrane alignment of the pore ...... solid-state NMR spectroscopy.
@en
type
label
Membrane alignment of the pore-forming component TatA
@nl
Membrane alignment of the pore ...... solid-state NMR spectroscopy.
@en
prefLabel
Membrane alignment of the pore-forming component TatA
@nl
Membrane alignment of the pore ...... solid-state NMR spectroscopy.
@en
P2093
P356
P1476
Membrane alignment of the pore ...... solid-state NMR spectroscopy.
@en
P2093
Nadine Roth
Stephan L Grage
Torsten H Walther
P304
15945-15956
P356
10.1021/JA106963S
P407
P577
2010-10-26T00:00:00Z