This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.

2lzr

From Proteopedia

(Difference between revisions)

Jump to: navigation, search

Revision as of 22:15, 25 December 2014

TatA T22P

Structural highlights

2lzr is a 1 chain structure with sequence from Escherichia coli k-12. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
NonStd Res:
Gene:	b3836, JW3813, mttA1, tatA, yigT (Escherichia coli K-12)
Resources:	FirstGlance, OCA, RCSB, PDBsum

Function

[TATA_ECOLI] 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.^[1] ^[2]

Publication Abstract from PubMed

The twin-arginine translocase (Tat) carries out the remarkable process of translocating fully folded proteins across the cytoplasmic membrane of prokaryotes and the thylakoid membrane of plant chloroplasts. Tat is required for bacterial pathogenesis and for photosynthesis in plants. TatA, the protein-translocating element of the Tat system, is a small transmembrane protein that assembles into ring-like oligomers of variable size. We have determined a structural model of the Escherichia coli TatA complex in detergent solution by NMR. TatA assembly is mediated entirely by the transmembrane helix. The amphipathic helix extends outwards from the ring of transmembrane helices, permitting assembly of complexes with variable subunit numbers. Transmembrane residue Gln8 points inward, resulting in a short hydrophobic pore in the center of the complex. Simulations of the TatA complex in lipid bilayers indicate that the short transmembrane domain distorts the membrane. This finding suggests that TatA facilitates protein transport by sensitizing the membrane to transient rupture.

Structural model for the protein-translocating element of the twin-arginine transport system.,Rodriguez F, Rouse SL, Tait CE, Harmer J, De Riso A, Timmel CR, Sansom MS, Berks BC, Schnell JR Proc Natl Acad Sci U S A. 2013 Mar 7. PMID:23471988^[3]

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

References

↑ Sargent F, Bogsch EG, Stanley NR, Wexler M, Robinson C, Berks BC, Palmer T. Overlapping functions of components of a bacterial Sec-independent protein export pathway. EMBO J. 1998 Jul 1;17(13):3640-50. PMID:9649434 doi:10.1093/emboj/17.13.3640
↑ Ize B, Gerard F, Zhang M, Chanal A, Voulhoux R, Palmer T, Filloux A, Wu LF. In vivo dissection of the Tat translocation pathway in Escherichia coli. J Mol Biol. 2002 Mar 29;317(3):327-35. PMID:11922668 doi:10.1006/jmbi.2002.5431
↑ Rodriguez F, Rouse SL, Tait CE, Harmer J, De Riso A, Timmel CR, Sansom MS, Berks BC, Schnell JR. Structural model for the protein-translocating element of the twin-arginine transport system. Proc Natl Acad Sci U S A. 2013 Mar 7. PMID:23471988 doi:http://dx.doi.org/10.1073/pnas.1219486110

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

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

@@ Line 7: / Line 7: @@
 <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=2lzr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2lzr OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2lzr RCSB], [http://www.ebi.ac.uk/pdbsum/2lzr PDBsum]</span></td></tr>
 </table>
+== Function ==
+[[http://www.uniprot.org/uniprot/TATA_ECOLI TATA_ECOLI]] 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.<ref>PMID:9649434</ref> <ref>PMID:11922668</ref>
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==

2lzr

From Proteopedia

Revision as of 22:15, 25 December 2014

TatA T22P

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

Personal tools

Navigation

Search

Toolbox