2l16

From Proteopedia

(Difference between revisions)

Revision as of 08:27, 25 July 2018

Solution structure of Bacillus subtilits TatAd protein in DPC micelles

Structural highlights

2l16 is a 1 chain structure with sequence from "vibrio_subtilis"_ehrenberg_1835 "vibrio subtilis" ehrenberg 1835. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Gene:	tatAd, yczB, BSU02630 ("Vibrio subtilis" Ehrenberg 1835)
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[TATAD_BACSU] Part of the twin-arginine translocation (Tat) system that transports large folded proteins containing a characteristic twin-arginine motif in their signal peptide across membranes. TatA could form the protein-conducting channel of the Tat system. Required for PhoD secretion. The cytosolic fraction of TatAd binds the precursor of PhoD.[HAMAP-Rule:MF_00236]^[1]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

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.

Solution NMR Structure of the TatA Component of the Twin-Arginine Protein Transport System from Gram-Positive Bacterium Bacillus subtilis.,Hu Y, Zhao E, Li H, Xia B, Jin C J Am Chem Soc. 2010 Aug 20. PMID:20726548^[2]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Barnett JP, Eijlander RT, Kuipers OP, Robinson C. A minimal Tat system from a gram-positive organism: a bifunctional TatA subunit participates in discrete TatAC and TatA complexes. J Biol Chem. 2008 Feb 1;283(5):2534-42. Epub 2007 Nov 20. PMID:18029357 doi:http://dx.doi.org/10.1074/jbc.M708134200
↑ Hu Y, Zhao E, Li H, Xia B, Jin C. Solution 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. PMID:20726548 doi:10.1021/ja1053785

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2l16"

Categories: Vibrio subtilis ehrenberg 1835 | Hu, Y | Jin, C | Membrane protein | Protein transport

@@ Line 1: / Line 1: @@
 ==Solution structure of Bacillus subtilits TatAd protein in DPC micelles==
 <StructureSection load='2l16' size='340' side='right' caption='[[2l16]], [[NMR_Ensembles_of_Models | 40 NMR models]]' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[2l16]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_globigii"_migula_1900 "bacillus globigii" migula 1900]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2L16 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2L16 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[2l16]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"vibrio_subtilis"_ehrenberg_1835 "vibrio subtilis" ehrenberg 1835]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2L16 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2L16 FirstGlance]. <br>
-</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">tatAd, yczB, BSU02630 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1423 "Bacillus globigii" Migula 1900])</td></tr>
+</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">tatAd, yczB, BSU02630 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1423 "Vibrio subtilis" Ehrenberg 1835])</td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2l16 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2l16 OCA], [http://pdbe.org/2l16 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2l16 RCSB], [http://www.ebi.ac.uk/pdbsum/2l16 PDBsum]</span></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2l16 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2l16 OCA], [http://pdbe.org/2l16 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2l16 RCSB], [http://www.ebi.ac.uk/pdbsum/2l16 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2l16 ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 12: / Line 13: @@
 Check<jmol>
   <jmolCheckbox>
-    <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/l1/2l16_consurf.spt"</scriptWhenChecked>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/l1/2l16_consurf.spt"</scriptWhenChecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>
   </jmolCheckbox>
-</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/chain_selection.php?pdb_ID=2ata ConSurf].
+</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2l16 ConSurf].
 <div style="clear:both"></div>
 <div style="background-color:#fffaf0;">
@@ Line 31: / Line 32: @@
 __TOC__
 </StructureSection>
-[[Category: Bacillus globigii migula 1900]]
+[[Category: Vibrio subtilis ehrenberg 1835]]
 [[Category: Hu, Y]]
 [[Category: Jin, C]]
 [[Category: Membrane protein]]
 [[Category: Protein transport]]

2l16

From Proteopedia

Revision as of 08:27, 25 July 2018

Solution structure of Bacillus subtilits TatAd protein in DPC micelles

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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