Related ArticlesSolution NMR Structure of the TatA Component of the Twin-Arginine Protein Transport System from Gram-Positive Bacterium Bacillus subtilis.
J Am Chem Soc. 2010 Aug 20;
Authors: Hu Y, Zhao E, Li H, Xia B, Jin C
The twin-arginine transport (Tat) system translocates folded proteins across the bacterial cytoplasmic or chloroplast thylakoid membrane of plants. The Tat system in most Gram-positive bacteria consists of two essential components, the TatA and TatC proteins. TatA is considered to be a bifunctional subunit, which can form a protein-conducting channel by self-oligomerization and can also participate in substrate recognition. However, the molecular mechanism underlying protein translocation remains elusive. Herein, we report the solution structure of the TatA(d) protein from Bacillus subtilis by NMR spectroscopy, the first structure of the Tat system at atomic resolution. TatA(d) shows an L-shaped structure formed by a transmembrane helix and an amphipathic helix, while the C-terminal tail is largely unstructured. Our results strongly support the postulated topology of TatA(d) in which the transmembrane helix is inserted into the lipid bilayer while the amphipathic helix lies at the membrane-water interface. Moreover, the structure of TatA(d) revealed the structural importance of several conserved residues at the hinge region, thus shedding new light on further elucidation of the protein transport mechanism of the Tat system.
PMID: 20726548 [PubMed - as supplied by publisher]
[NMR paper] The NMR structure of the sensory domain of the membranous two-component fumarate sens
The NMR structure of the sensory domain of the membranous two-component fumarate sensor (histidine protein kinase) DcuS of Escherichia coli.
The NMR structure of the sensory domain of the membranous two-component fumarate sensor (histidine protein kinase) DcuS of Escherichia coli.
J Biol Chem. 2003 Oct 3;278(40):39185-8
Authors: Pappalardo L, Janausch IG, Vijayan V, Zientz E, Junker J, Peti W, Zweckstetter M, Unden G, Griesinger C
The structure of the water-soluble, periplasmic domain of the fumarate sensor DcuS (DcuS-pd) has been determined...
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Membrane Alignment of the Pore-Forming Component TatA(d) of the Twin-Arginine Translo
Membrane Alignment of the Pore-Forming Component TatA(d) of the Twin-Arginine Translocase from Bacillus subtilis Resolved by Solid-State NMR Spectroscopy.
Related Articles Membrane Alignment of the Pore-Forming Component TatA(d) of the Twin-Arginine Translocase from Bacillus subtilis Resolved by Solid-State NMR Spectroscopy.
J Am Chem Soc. 2010 Oct 26;
Authors: Walther TH, Grage SL, Roth N, Ulrich AS
The twin-arginine translocase (Tat) provides protein export in bacteria and plant chloroplasts and is capable of transporting fully folded...
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Membrane Alignment of the Pore-Forming Component TatAd of the Twin-Arginine Transloca
Membrane Alignment of the Pore-Forming Component TatAd of the Twin-Arginine Translocase from Bacillus subtilis Resolved by Solid-State NMR Spectroscopy
Torsten H. Walther, Stephan L. Grage, Nadine Roth and Anne S. Ulrich
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/ja106963s/aop/images/medium/ja-2010-06963s_0001.gif
Journal of the American Chemical Society
DOI: 10.1021/ja106963s
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[NMR paper] Solution structure of phenol hydroxylase protein component P2 determined by NMR spect
Solution structure of phenol hydroxylase protein component P2 determined by NMR spectroscopy.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--pubs.acs.org-images-acspubs.jpg Related Articles Solution structure of phenol hydroxylase protein component P2 determined by NMR spectroscopy.
Biochemistry. 1997 Jan 21;36(3):495-504
Authors: Qian H, Edlund U, Powlowski J, Shingler V, Sethson I
Phenol hydroxylase from Pseudomonas sp. CF600 is a member of a family of binuclear iron-center-containing multicomponent oxygenases, which catalyzes the...
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[NMR paper] Solution structure of phenol hydroxylase protein component P2 determined by NMR spect
Solution structure of phenol hydroxylase protein component P2 determined by NMR spectroscopy.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--pubs.acs.org-images-acspubs.jpg Related Articles Solution structure of phenol hydroxylase protein component P2 determined by NMR spectroscopy.
Biochemistry. 1997 Jan 21;36(3):495-504
Authors: Qian H, Edlund U, Powlowski J, Shingler V, Sethson I
Phenol hydroxylase from Pseudomonas sp. CF600 is a member of a family of binuclear iron-center-containing multicomponent oxygenases, which catalyzes the...
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[NMR paper] Na(+)-H+ and Na(+)-Li+ exchange are mediated by the same membrane transport protein i
Na(+)-H+ and Na(+)-Li+ exchange are mediated by the same membrane transport protein in human red blood cells: an NMR investigation.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--pubs.acs.org-images-acspubs.jpg Related Articles Na(+)-H+ and Na(+)-Li+ exchange are mediated by the same membrane transport protein in human red blood cells: an NMR investigation.
Biochemistry. 1996 Sep 24;35(38):12433-42
Authors: Chi Y, Mo S, Mota de Freitas D
Na(+)-H+ exchange is a transport system present in erythrocytes which plays an important role in...
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[NMR paper] Solution structure of component B from methane monooxygenase derived through heteronu
Solution structure of component B from methane monooxygenase derived through heteronuclear NMR and molecular modeling.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--pubs.acs.org-images-acspubs.jpg Related Articles Solution structure of component B from methane monooxygenase derived through heteronuclear NMR and molecular modeling.
Biochemistry. 1999 May 4;38(18):5799-812
Authors: Chang SL, Wallar BJ, Lipscomb JD, Mayo KH
Methane monooxygenase (MMO) is a nonheme iron-containing enzyme which consists of three protein components: a...
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Solution NMR Structure of the TatA Component of the Twin-Arginine Protein Transport S
Solution NMR Structure of the TatA Component of the Twin-Arginine Protein Transport System from Gram-Positive Bacterium Bacillus subtilis
Yunfei Hu et al
http://pubs.acs.org//appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/ja1053785/aop/images/medium/ja-2010-053785_0001.gifJournal of the American Chemical Society, Volume 0, Issue 0, Articles ASAP (As Soon As Publishable).
Source: Journal of the American Chemical Society