9r91: Difference between revisions

Latest revision as of 04:58, 27 May 2026

Trimer TatBC complex with bound substrate SufI

Structural highlights

9r91 is a 7 chain structure with sequence from Escherichia coli. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	Electron Microscopy, Resolution 3.7Å
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

TATC_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. Together with TatB, TatC is part of a receptor directly interacting with Tat signal peptides.[HAMAP-Rule:MF_00902]^[1] ^[2] ^[3] ^[4] ^[5]

References

↑ 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
↑ Alami M, Lüke I, Deitermann S, Eisner G, Koch HG, Brunner J, Müller M. Differential interactions between a twin-arginine signal peptide and its translocase in Escherichia coli. Mol Cell. 2003 Oct;12(4):937-46. PMID:14580344 doi:10.1016/s1097-2765(03)00398-8
↑ Tarry MJ, Schäfer E, Chen S, Buchanan G, Greene NP, Lea SM, Palmer T, Saibil HR, Berks BC. Structural analysis of substrate binding by the TatBC component of the twin-arginine protein transport system. Proc Natl Acad Sci U S A. 2009 Aug 11;106(32):13284-9. PMID:19666509 doi:10.1073/pnas.0901566106
↑ Maurer C, Panahandeh S, Jungkamp AC, Moser M, Müller M. TatB functions as an oligomeric binding site for folded Tat precursor proteins. Mol Biol Cell. 2010 Dec;21(23):4151-61. PMID:20926683 doi:10.1091/mbc.E10-07-0585
↑ Bogsch EG, Sargent F, Stanley NR, Berks BC, Robinson C, Palmer T. An essential component of a novel bacterial protein export system with homologues in plastids and mitochondria. J Biol Chem. 1998 Jul 17;273(29):18003-6. PMID:9660752 doi:10.1074/jbc.273.29.18003

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OCA

[1] 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

[2] Alami M, Lüke I, Deitermann S, Eisner G, Koch HG, Brunner J, Müller M. Differential interactions between a twin-arginine signal peptide and its translocase in Escherichia coli. Mol Cell. 2003 Oct;12(4):937-46. PMID:14580344 doi:10.1016/s1097-2765(03)00398-8

[3] Tarry MJ, Schäfer E, Chen S, Buchanan G, Greene NP, Lea SM, Palmer T, Saibil HR, Berks BC. Structural analysis of substrate binding by the TatBC component of the twin-arginine protein transport system. Proc Natl Acad Sci U S A. 2009 Aug 11;106(32):13284-9. PMID:19666509 doi:10.1073/pnas.0901566106

[4] Maurer C, Panahandeh S, Jungkamp AC, Moser M, Müller M. TatB functions as an oligomeric binding site for folded Tat precursor proteins. Mol Biol Cell. 2010 Dec;21(23):4151-61. PMID:20926683 doi:10.1091/mbc.E10-07-0585

[5] Bogsch EG, Sargent F, Stanley NR, Berks BC, Robinson C, Palmer T. An essential component of a novel bacterial protein export system with homologues in plastids and mitochondria. J Biol Chem. 1998 Jul 17;273(29):18003-6. PMID:9660752 doi:10.1074/jbc.273.29.18003

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@@ Line 1: / Line 1: @@
-'''Unreleased structure'''
-The entry 9r91 is ON HOLD  until Paper Publication
+==Trimer TatBC complex with bound substrate SufI==
+<StructureSection load='9r91' size='340' side='right'caption='[[9r91]], [[Resolution|resolution]] 3.70&Aring;' scene=''>
-Authors:
+== Structural highlights ==
+<table><tr><td colspan='2'>[[9r91]] is a 7 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=9R91 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=9R91 FirstGlance]. <br>
-Description:
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 3.7&#8491;</td></tr>
-[[Category: Unreleased Structures]]
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=9r91 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=9r91 OCA], [https://pdbe.org/9r91 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=9r91 RCSB], [https://www.ebi.ac.uk/pdbsum/9r91 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=9r91 ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/TATC_ECOLI TATC_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. Together with TatB, TatC is part of a receptor directly interacting with Tat signal peptides.[HAMAP-Rule:MF_00902]<ref>PMID:11922668</ref> <ref>PMID:14580344</ref> <ref>PMID:19666509</ref> <ref>PMID:20926683</ref> <ref>PMID:9660752</ref>
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Escherichia coli]]
+[[Category: Large Structures]]
+[[Category: Sazanov L]]
+[[Category: Zhao Z]]

9r91: Difference between revisions

Latest revision as of 04:58, 27 May 2026

Trimer TatBC complex with bound substrate SufI

Structural highlights

Function

References

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