2mi2 - Revision history

OCA at 06:05, 15 May 2024

2024-05-15T06:05:48Z

← Older revision		Revision as of 06:05, 15 May 2024
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	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[2mi2]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2MI2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2MI2 FirstGlance]. <br>		<table><tr><td colspan='2'>[[2mi2]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2MI2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2MI2 FirstGlance]. <br>
	</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2mi2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2mi2 OCA], [https://pdbe.org/2mi2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2mi2 RCSB], [https://www.ebi.ac.uk/pdbsum/2mi2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2mi2 ProSAT]</span></td></tr>		</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models\|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
			<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2mi2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2mi2 OCA], [https://pdbe.org/2mi2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2mi2 RCSB], [https://www.ebi.ac.uk/pdbsum/2mi2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2mi2 ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==

OCA at 09:36, 14 June 2023

2023-06-14T09:36:04Z

← Older revision		Revision as of 09:36, 14 June 2023
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	<StructureSection load='2mi2' size='340' side='right'caption='[[2mi2]]' scene=''>		<StructureSection load='2mi2' size='340' side='right'caption='[[2mi2]]' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>Full ~~crystallographic~~ information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2MI2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2MI2 FirstGlance]. <br>		<table><tr><td colspan='2'>[[2mi2]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2MI2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2MI2 FirstGlance]. <br>
	</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2mi2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2mi2 OCA], [https://pdbe.org/2mi2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2mi2 RCSB], [https://www.ebi.ac.uk/pdbsum/2mi2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2mi2 ProSAT]</span></td></tr>		</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2mi2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2mi2 OCA], [https://pdbe.org/2mi2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2mi2 RCSB], [https://www.ebi.ac.uk/pdbsum/2mi2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2mi2 ProSAT]</span></td></tr>
	</table>		</table>
			== Function ==
			[https://www.uniprot.org/uniprot/A0A0D8VEJ4_ECOLX A0A0D8VEJ4_ECOLX] 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 TatC, TatB is part of a receptor directly interacting with Tat signal peptides. TatB may form an oligomeric binding site that transiently accommodates folded Tat precursor proteins before their translocation.[HAMAP-Rule:MF_00237]
			<div style="background-color:#fffaf0;">
			== Publication Abstract from PubMed ==
			The twin-arginine protein transport (Tat) system translocates fully folded proteins across lipid membranes. In Escherichia coli, the Tat system comprises three essential components: TatA, TatB and TatC. The protein translocation process is proposed to initiate by signal peptide recognition and substrate binding to the TatBC complex. Upon formation of the TatBC-substrate protein complex, the TatA subunits are recruited and form the protein translocation pore. Experimental evidences suggest that TatB forms a tight complex with TatC at 1:1 molar ratio and the TatBC complex contains multiple copies of both proteins. Cross-linking experiments demonstrate that TatB functions in tetrameric units and interacts with both TatC and substrate proteins. However, structural information of the TatB protein is still lacking, and its functional mechanism remains elusive. Herein, we report the solution structure of TatB in DPC micelles determined by Nuclear Magnetic Resonance (NMR) spectroscopy. Overall, the structure shows an extended 'L-shape' conformation comprising four helices: a transmembrane helix (TMH) alpha1, an amphipathic helix (APH) alpha2, and two solvent exposed helices alpha3 and alpha4. The packing of TMH and APH is relatively rigid, whereas helices alpha3 and alpha4 display notably higher mobility. The observed floppiness of helices alpha3 and alpha4 allows TatB to sample a large conformational space, thus providing high structural plasticity to interact with substrate proteins of different sizes and shapes.

			Solution structure of the TatB component of the twin-arginine translocation system.,Zhang Y, Wang L, Hu Y, Jin C Biochim Biophys Acta. 2014 Mar 31;1838(7):1881-1888. doi:, 10.1016/j.bbamem.2014.03.015. PMID:24699374<ref>PMID:24699374</ref>

			From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
			</div>
			<div class="pdbe-citations 2mi2" style="background-color:#fffaf0;"></div>
			== References ==
			<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
			[[Category: Escherichia coli]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
	[[Category: Hu Y]]		[[Category: Hu Y]]

OCA at 10:21, 31 August 2022

2022-08-31T10:21:51Z

← Older revision		Revision as of 10:21, 31 August 2022
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	==Solution structure of the E. coli TatB protein in DPC micelles==		==Solution structure of the E. coli TatB protein in DPC micelles==
	<StructureSection load='2mi2' size='340' side='right'caption='[[2mi2~~]], [[NMR_Ensembles_of_Models \| 15 NMR models~~]]' scene=''>		<StructureSection load='2mi2' size='340' side='right'caption='[[2mi2]]' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>~~[[2mi2]] is a 1 chain structure.~~ Full ~~experimental~~ information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2MI2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2MI2 FirstGlance]. <br>		<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2MI2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2MI2 FirstGlance]. <br>
	</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2mi2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2mi2 OCA], [https://pdbe.org/2mi2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2mi2 RCSB], [https://www.ebi.ac.uk/pdbsum/2mi2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2mi2 ProSAT]</span></td></tr>		</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2mi2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2mi2 OCA], [https://pdbe.org/2mi2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2mi2 RCSB], [https://www.ebi.ac.uk/pdbsum/2mi2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2mi2 ProSAT]</span></td></tr>
	</table>		</table>
	~~== Function ==~~
	[[https://www.uniprot.org/uniprot/E2QI32_ECOLX E2QI32_ECOLX]] 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 TatC, TatB is part of a receptor directly interacting with Tat signal peptides. TatB may form an oligomeric binding site that transiently accommodates folded Tat precursor proteins before their translocation (By similarity).[HAMAP-Rule:MF_00237][SAAS:SAAS003998_004_091047]
	~~<div style="background-color:#fffaf0;">~~
	~~== Publication Abstract from PubMed ==~~
	The twin-arginine protein transport (Tat) system translocates fully folded proteins across lipid membranes. In Escherichia coli, the Tat system comprises three essential components: TatA, TatB and TatC. The protein translocation process is proposed to initiate by signal peptide recognition and substrate binding to the TatBC complex. Upon formation of the TatBC-substrate protein complex, the TatA subunits are recruited and form the protein translocation pore. Experimental evidences suggest that TatB forms a tight complex with TatC at 1:1 molar ratio and the TatBC complex contains multiple copies of both proteins. Cross-linking experiments demonstrate that TatB functions in tetrameric units and interacts with both TatC and substrate proteins. However, structural information of the TatB protein is still lacking, and its functional mechanism remains elusive. Herein, we report the solution structure of TatB in DPC micelles determined by Nuclear Magnetic Resonance (NMR) spectroscopy. Overall, the structure shows an extended 'L-shape' conformation comprising four helices: a transmembrane helix (TMH) alpha1, an amphipathic helix (APH) alpha2, and two solvent exposed helices alpha3 and alpha4. The packing of TMH and APH is relatively rigid, whereas helices alpha3 and alpha4 display notably higher mobility. The observed floppiness of helices alpha3 and alpha4 allows TatB to sample a large conformational space, thus providing high structural plasticity to interact with substrate proteins of different sizes and shapes.

	Solution structure of the TatB component of the twin-arginine translocation system.,Zhang Y, Wang L, Hu Y, Jin C Biochim Biophys Acta. 2014 Mar 31;1838(7):1881-1888. doi:, 10.1016/j.bbamem.2014.03.015. PMID:24699374<ref>PMID:24699374</ref>

	~~From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>~~
	~~</div>~~
	~~<div class="pdbe-citations 2mi2" style="background-color:#fffaf0;"></div>~~
	~~== References ==~~
	~~<references/>~~
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
	[[Category: Large Structures]]		[[Category: Large Structures]]
	[[Category: Hu, Y]]		[[Category: Hu Y]]
	[[Category: Jin, C]]		[[Category: Jin C]]
	[[Category: Wang, L]]		[[Category: Wang L]]
	[[Category: Zhang, Y]]		[[Category: Zhang Y]]
	~~[[Category: Transport protein~~]]

OCA at 04:54, 25 August 2022

2022-08-25T04:54:50Z

← Older revision		Revision as of 04:54, 25 August 2022
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	<StructureSection load='2mi2' size='340' side='right'caption='[[2mi2]], [[NMR_Ensembles_of_Models \| 15 NMR models]]' scene=''>		<StructureSection load='2mi2' size='340' side='right'caption='[[2mi2]], [[NMR_Ensembles_of_Models \| 15 NMR models]]' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[2mi2]] is a 1 chain structure ~~with sequence from [https://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895]~~. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2MI2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2MI2 FirstGlance]. <br>		<table><tr><td colspan='2'>[[2mi2]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2MI2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2MI2 FirstGlance]. <br>
	</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">tatB, LF82_2221 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 "Bacillus coli" Migula 1895])</td></tr>		</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2mi2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2mi2 OCA], [https://pdbe.org/2mi2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2mi2 RCSB], [https://www.ebi.ac.uk/pdbsum/2mi2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2mi2 ProSAT]</span></td></tr>
	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2mi2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2mi2 OCA], [https://pdbe.org/2mi2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2mi2 RCSB], [https://www.ebi.ac.uk/pdbsum/2mi2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2mi2 ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
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	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
	~~[[Category: Bacillus coli migula 1895]]~~
	[[Category: Large Structures]]		[[Category: Large Structures]]
	[[Category: Hu, Y]]		[[Category: Hu, Y]]

OCA at 15:15, 2 June 2021

2021-06-02T15:15:08Z

← Older revision		Revision as of 15:15, 2 June 2021
Line 1:		Line 1:

	==Solution structure of the E. coli TatB protein in DPC micelles==		==Solution structure of the E. coli TatB protein in DPC micelles==
	<StructureSection load='2mi2' size='340' side='right' caption='[[2mi2]], [[NMR_Ensembles_of_Models \| 15 NMR models]]' scene=''>		<StructureSection load='2mi2' size='340' side='right'caption='[[2mi2]], [[NMR_Ensembles_of_Models \| 15 NMR models]]' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[2mi2]] is a 1 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2MI2 OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=2MI2 FirstGlance]. <br>		<table><tr><td colspan='2'>[[2mi2]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2MI2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2MI2 FirstGlance]. <br>
	</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">tatB, LF82_2221 ([~~http~~://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 "Bacillus coli" Migula 1895])</td></tr>		</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">tatB, LF82_2221 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 "Bacillus coli" Migula 1895])</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=2mi2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2mi2 OCA], [~~http~~://pdbe.org/2mi2 PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=2mi2 RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/2mi2 PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=2mi2 ProSAT]</span></td></tr>		<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2mi2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2mi2 OCA], [https://pdbe.org/2mi2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2mi2 RCSB], [https://www.ebi.ac.uk/pdbsum/2mi2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2mi2 ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
	[[~~http~~://www.uniprot.org/uniprot/E2QI32_ECOLX E2QI32_ECOLX]] 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 TatC, TatB is part of a receptor directly interacting with Tat signal peptides. TatB may form an oligomeric binding site that transiently accommodates folded Tat precursor proteins before their translocation (By similarity).[HAMAP-Rule:MF_00237][SAAS:SAAS003998_004_091047]		[[https://www.uniprot.org/uniprot/E2QI32_ECOLX E2QI32_ECOLX]] 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 TatC, TatB is part of a receptor directly interacting with Tat signal peptides. TatB may form an oligomeric binding site that transiently accommodates folded Tat precursor proteins before their translocation (By similarity).[HAMAP-Rule:MF_00237][SAAS:SAAS003998_004_091047]
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 23:		Line 23:
	</StructureSection>		</StructureSection>
	[[Category: Bacillus coli migula 1895]]		[[Category: Bacillus coli migula 1895]]
			[[Category: Large Structures]]
	[[Category: Hu, Y]]		[[Category: Hu, Y]]
	[[Category: Jin, C]]		[[Category: Jin, C]]

OCA at 23:07, 9 August 2018

2018-08-09T23:07:39Z

← Older revision		Revision as of 23:07, 9 August 2018
Line 1:		Line 1:

	==Solution structure of the E. coli TatB protein in DPC micelles==		==Solution structure of the E. coli TatB protein in DPC micelles==
	<StructureSection load='2mi2' size='340' side='right' caption='[[2mi2]], [[NMR_Ensembles_of_Models \| 15 NMR models]]' scene=''>		<StructureSection load='2mi2' size='340' side='right' caption='[[2mi2]], [[NMR_Ensembles_of_Models \| 15 NMR models]]' scene=''>
Line 4:		Line 5:
	<table><tr><td colspan='2'>[[2mi2]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2MI2 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2MI2 FirstGlance]. <br>		<table><tr><td colspan='2'>[[2mi2]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2MI2 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2MI2 FirstGlance]. <br>
	</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">tatB, LF82_2221 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 "Bacillus coli" Migula 1895])</td></tr>		</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">tatB, LF82_2221 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 "Bacillus coli" Migula 1895])</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=2mi2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2mi2 OCA], [http://pdbe.org/2mi2 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2mi2 RCSB], [http://www.ebi.ac.uk/pdbsum/2mi2 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=2mi2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2mi2 OCA], [http://pdbe.org/2mi2 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2mi2 RCSB], [http://www.ebi.ac.uk/pdbsum/2mi2 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2mi2 ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==

OCA at 17:22, 10 September 2015

2015-09-10T17:22:22Z

← Older revision		Revision as of 17:22, 10 September 2015
Line 4:		Line 4:
	<table><tr><td colspan='2'>[[2mi2]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2MI2 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2MI2 FirstGlance]. <br>		<table><tr><td colspan='2'>[[2mi2]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2MI2 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2MI2 FirstGlance]. <br>
	</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">tatB, LF82_2221 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 "Bacillus coli" Migula 1895])</td></tr>		</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">tatB, LF82_2221 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 "Bacillus coli" Migula 1895])</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=2mi2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2mi2 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2mi2 RCSB], [http://www.ebi.ac.uk/pdbsum/2mi2 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=2mi2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2mi2 OCA], [http://pdbe.org/2mi2 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2mi2 RCSB], [http://www.ebi.ac.uk/pdbsum/2mi2 PDBsum]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
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	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>		From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
	</div>		</div>
			<div class="pdbe-citations 2mi2" style="background-color:#fffaf0;"></div>
	== References ==		== References ==
	<references/>		<references/>

OCA at 03:33, 25 December 2014

2014-12-25T03:33:08Z

← Older revision		Revision as of 03:33, 25 December 2014
Line 2:		Line 2:
	<StructureSection load='2mi2' size='340' side='right' caption='[[2mi2]], [[NMR_Ensembles_of_Models \| 15 NMR models]]' scene=''>		<StructureSection load='2mi2' size='340' side='right' caption='[[2mi2]], [[NMR_Ensembles_of_Models \| 15 NMR models]]' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[2mi2]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2MI2 OCA]. <br>		<table><tr><td colspan='2'>[[2mi2]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2MI2 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2MI2 FirstGlance]. <br>
	</td></tr><tr><td class="sblockLbl"><b>~~Activity~~:</b></td><td class="sblockDat">~~<span class='plainlinks'>~~[http://en.~~wikipedia~~.~~org/wiki/Glucokinase Glucokinase], with EC number [http://www~~.~~brenda-enzymes~~.~~info~~/~~php~~/~~result_flat~~.~~php4~~?~~ecno~~=~~2.7.1.2 2.7.1.2~~] ~~</span>~~</td></tr>		</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">tatB, LF82_2221 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 "Bacillus coli" Migula 1895])</td></tr>
	<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2mi2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2mi2 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2mi2 RCSB], [http://www.ebi.ac.uk/pdbsum/2mi2 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=2mi2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2mi2 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2mi2 RCSB], [http://www.ebi.ac.uk/pdbsum/2mi2 PDBsum]</span></td></tr>
	<table>		</table>
			== Function ==
			[[http://www.uniprot.org/uniprot/E2QI32_ECOLX E2QI32_ECOLX]] 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 TatC, TatB is part of a receptor directly interacting with Tat signal peptides. TatB may form an oligomeric binding site that transiently accommodates folded Tat precursor proteins before their translocation (By similarity).[HAMAP-Rule:MF_00237][SAAS:SAAS003998_004_091047]
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 12:		Line 14:
	Solution structure of the TatB component of the twin-arginine translocation system.,Zhang Y, Wang L, Hu Y, Jin C Biochim Biophys Acta. 2014 Mar 31;1838(7):1881-1888. doi:, 10.1016/j.bbamem.2014.03.015. PMID:24699374<ref>PMID:24699374</ref>		Solution structure of the TatB component of the twin-arginine translocation system.,Zhang Y, Wang L, Hu Y, Jin C Biochim Biophys Acta. 2014 Mar 31;1838(7):1881-1888. doi:, 10.1016/j.bbamem.2014.03.015. PMID:24699374<ref>PMID:24699374</ref>

	From ~~MEDLINEÂ®~~/~~PubMedÂ®~~, a database of the U.S. National Library of Medicine.<br>		From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
	</div>		</div>
	== References ==		== References ==
Line 18:		Line 20:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
	[[Category: Hu, Y.]]		[[Category: Bacillus coli migula 1895]]
	[[Category: Jin, C.]]		[[Category: Hu, Y]]
	[[Category: Wang, L.]]		[[Category: Jin, C]]
	[[Category: Zhang, Y.]]		[[Category: Wang, L]]
			[[Category: Zhang, Y]]
	[[Category: Transport protein]]		[[Category: Transport protein]]

OCA at 09:21, 1 May 2014

2014-05-01T09:21:56Z

← Older revision		Revision as of 09:21, 1 May 2014
Line 13:		Line 13:

	From MEDLINEÂ®/PubMedÂ®, a database of the U.S. National Library of Medicine.<br>		From MEDLINEÂ®/PubMedÂ®, a database of the U.S. National Library of Medicine.<br>
	</div>== References ==		</div>
			== References ==
	<references/>		<references/>
	__TOC__		__TOC__

OCA at 09:18, 1 May 2014

2014-05-01T09:18:06Z

← Older revision		Revision as of 09:18, 1 May 2014
Line 2:		Line 2:
	<StructureSection load='2mi2' size='340' side='right' caption='[[2mi2]], [[NMR_Ensembles_of_Models \| 15 NMR models]]' scene=''>		<StructureSection load='2mi2' size='340' side='right' caption='[[2mi2]], [[NMR_Ensembles_of_Models \| 15 NMR models]]' scene=''>
	== Structural highlights ==		== Structural highlights ==
	[[2mi2]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2MI2 OCA]. <br>		<table><tr><td colspan='2'>[[2mi2]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2MI2 OCA]. <br>
	<b>Activity:</b> <span class='plainlinks'>[http://en.wikipedia.org/wiki/Glucokinase Glucokinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.2 2.7.1.2] </span><br>		</td></tr><tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Glucokinase Glucokinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.2 2.7.1.2] </span></td></tr>
	<b>Resources:</b> <span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2mi2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2mi2 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2mi2 RCSB], [http://www.ebi.ac.uk/pdbsum/2mi2 PDBsum]</span><br>		<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2mi2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2mi2 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2mi2 RCSB], [http://www.ebi.ac.uk/pdbsum/2mi2 PDBsum]</span></td></tr>
			<table>
			<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
	The twin-arginine protein transport (Tat) system translocates fully folded proteins across lipid membranes. In Escherichia coli, the Tat system comprises three essential components: TatA, TatB and TatC. The protein translocation process is proposed to initiate by signal peptide recognition and substrate binding to the TatBC complex. Upon formation of the TatBC-substrate protein complex, the TatA subunits are recruited and form the protein translocation pore. Experimental evidences suggest that TatB forms a tight complex with TatC at 1:1 molar ratio and the TatBC complex contains multiple copies of both proteins. Cross-linking experiments demonstrate that TatB functions in tetrameric units and interacts with both TatC and substrate proteins. However, structural information of the TatB protein is still lacking, and its functional mechanism remains elusive. Herein, we report the solution structure of TatB in DPC micelles determined by Nuclear Magnetic Resonance (NMR) spectroscopy. Overall, the structure shows an extended 'L-shape' conformation comprising four helices: a transmembrane helix (TMH) alpha1, an amphipathic helix (APH) alpha2, and two solvent exposed helices alpha3 and alpha4. The packing of TMH and APH is relatively rigid, whereas helices alpha3 and alpha4 display notably higher mobility. The observed floppiness of helices alpha3 and alpha4 allows TatB to sample a large conformational space, thus providing high structural plasticity to interact with substrate proteins of different sizes and shapes.		The twin-arginine protein transport (Tat) system translocates fully folded proteins across lipid membranes. In Escherichia coli, the Tat system comprises three essential components: TatA, TatB and TatC. The protein translocation process is proposed to initiate by signal peptide recognition and substrate binding to the TatBC complex. Upon formation of the TatBC-substrate protein complex, the TatA subunits are recruited and form the protein translocation pore. Experimental evidences suggest that TatB forms a tight complex with TatC at 1:1 molar ratio and the TatBC complex contains multiple copies of both proteins. Cross-linking experiments demonstrate that TatB functions in tetrameric units and interacts with both TatC and substrate proteins. However, structural information of the TatB protein is still lacking, and its functional mechanism remains elusive. Herein, we report the solution structure of TatB in DPC micelles determined by Nuclear Magnetic Resonance (NMR) spectroscopy. Overall, the structure shows an extended 'L-shape' conformation comprising four helices: a transmembrane helix (TMH) alpha1, an amphipathic helix (APH) alpha2, and two solvent exposed helices alpha3 and alpha4. The packing of TMH and APH is relatively rigid, whereas helices alpha3 and alpha4 display notably higher mobility. The observed floppiness of helices alpha3 and alpha4 allows TatB to sample a large conformational space, thus providing high structural plasticity to interact with substrate proteins of different sizes and shapes.
Line 11:		Line 13:

	From MEDLINEÂ®/PubMedÂ®, a database of the U.S. National Library of Medicine.<br>		From MEDLINEÂ®/PubMedÂ®, a database of the U.S. National Library of Medicine.<br>
	== References ==		</div>== References ==
	<references/>		<references/>
	__TOC__		__TOC__