4htt - Revision history

OCA at 11:44, 1 March 2024

2024-03-01T11:44:35Z

← Older revision		Revision as of 11:44, 1 March 2024
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	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[4htt]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Aquifex_aeolicus_VF5 Aquifex aeolicus VF5] and [https://en.wikipedia.org/wiki/Escherichia_virus_T4 Escherichia virus T4]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4HTT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4HTT FirstGlance]. <br>		<table><tr><td colspan='2'>[[4htt]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Aquifex_aeolicus_VF5 Aquifex aeolicus VF5] and [https://en.wikipedia.org/wiki/Escherichia_virus_T4 Escherichia virus T4]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4HTT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4HTT 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=4htt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4htt OCA], [https://pdbe.org/4htt PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4htt RCSB], [https://www.ebi.ac.uk/pdbsum/4htt PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4htt ProSAT]</span></td></tr>		</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models\|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution\|Resolution]] 6.8Å</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=4htt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4htt OCA], [https://pdbe.org/4htt PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4htt RCSB], [https://www.ebi.ac.uk/pdbsum/4htt PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4htt ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
	[https://www.uniprot.org/uniprot/ENLYS_BPT4 ENLYS_BPT4] Endolysin with lysozyme activity that degrades host peptidoglycans and participates with the holin and spanin proteins in the sequential events which lead to the programmed host cell lysis releasing the mature viral particles. Once the holin has permeabilized the host cell membrane, the endolysin can reach the periplasm and break down the peptidoglycan layer.<ref>PMID:22389108</ref> [https://www.uniprot.org/uniprot/TATC_AQUAE TATC_AQUAE] 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 (By similarity).		[https://www.uniprot.org/uniprot/ENLYS_BPT4 ENLYS_BPT4] Endolysin with lysozyme activity that degrades host peptidoglycans and participates with the holin and spanin proteins in the sequential events which lead to the programmed host cell lysis releasing the mature viral particles. Once the holin has permeabilized the host cell membrane, the endolysin can reach the periplasm and break down the peptidoglycan layer.<ref>PMID:22389108</ref> [https://www.uniprot.org/uniprot/TATC_AQUAE TATC_AQUAE] 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 (By similarity).
	~~<div style="background-color:#fffaf0;">~~
	~~== Publication Abstract from PubMed ==~~
	In bacteria, two signal-sequence-dependent secretion pathways translocate proteins across the cytoplasmic membrane. Although the mechanism of the ubiquitous general secretory pathway is becoming well understood, that of the twin-arginine translocation pathway, responsible for translocation of folded proteins across the bilayer, is more mysterious. TatC, the largest and most conserved of three integral membrane components, provides the initial binding site of the signal sequence prior to pore assembly. Here, we present two crystal structures of TatC from the thermophilic bacteria Aquifex aeolicus at 4.0 A and 6.8 A resolution. The membrane architecture of TatC includes a glove-shaped structure with a lipid-exposed pocket predicted by molecular dynamics to distort the membrane. Correlating the biochemical literature to these results suggests that the signal sequence binds in this pocket, leading to structural changes that facilitate higher order assemblies.

	The Glove-like Structure of the Conserved Membrane Protein TatC Provides Insight into Signal Sequence Recognition in Twin-Arginine Translocation.,Ramasamy S, Abrol R, Suloway CJ, Clemons WM Jr Structure. 2013 Apr 9. pii: S0969-2126(13)00085-3. doi:, 10.1016/j.str.2013.03.004. PMID:23583035<ref>PMID:23583035</ref>

	~~From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>~~
	~~</div>~~
	~~<div class="pdbe-citations 4htt" style="background-color:#fffaf0;"></div>~~
	== References ==		== References ==
	<references/>		<references/>

OCA at 08:13, 9 November 2022

2022-11-09T08:13:58Z

← Older revision		Revision as of 08:13, 9 November 2022
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	<StructureSection load='4htt' size='340' side='right'caption='[[4htt]], [[Resolution\|resolution]] 6.80Å' scene=''>		<StructureSection load='4htt' size='340' side='right'caption='[[4htt]], [[Resolution\|resolution]] 6.80Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[4htt]] is a 2 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/~~Bpt4 Bpt4~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4HTT OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=4HTT FirstGlance]. <br>		<table><tr><td colspan='2'>[[4htt]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Aquifex_aeolicus_VF5 Aquifex aeolicus VF5] and [https://en.wikipedia.org/wiki/Escherichia_virus_T4 Escherichia virus T4]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4HTT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4HTT FirstGlance]. <br>
	</td></tr>~~<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4hts\|4hts]]</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=4htt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4htt OCA], [https://pdbe.org/4htt PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4htt RCSB], [https://www.ebi.ac.uk/pdbsum/4htt PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4htt ProSAT]</span></td></tr>
	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">tatC, aq_1267, E ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10665 BPT4])</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Lysozyme Lysozyme], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.17 3.2.1.17] </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=4htt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4htt OCA], [~~http~~://pdbe.org/4htt PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=4htt RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/4htt PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=4htt ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
	[[~~http~~://www.uniprot.org/uniprot/TATC_AQUAE TATC_AQUAE]] 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 (By similarity).		[https://www.uniprot.org/uniprot/ENLYS_BPT4 ENLYS_BPT4] Endolysin with lysozyme activity that degrades host peptidoglycans and participates with the holin and spanin proteins in the sequential events which lead to the programmed host cell lysis releasing the mature viral particles. Once the holin has permeabilized the host cell membrane, the endolysin can reach the periplasm and break down the peptidoglycan layer.<ref>PMID:22389108</ref> [https://www.uniprot.org/uniprot/TATC_AQUAE TATC_AQUAE] 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 (By similarity).
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
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	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
	[[Category: ~~Bpt4~~]]		[[Category: Aquifex aeolicus VF5]]
			[[Category: Escherichia virus T4]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
	~~[[Category: Lysozyme]]~~		[[Category: Clemons Jr WM]]
	[[Category: Clemons~~, W M~~]]		[[Category: Ramasamy S]]
	[[Category: Ramasamy, S]]		[[Category: Suloway CJM]]
	[[Category: Suloway~~, C J.M]]~~
	~~[[Category: Hydrolase]]~~
	~~[[Category: Membrane]]~~
	~~[[Category: Twin arginine translocase receptor~~]]

OCA at 11:58, 17 July 2019

2019-07-17T11:58:04Z

← Older revision		Revision as of 11:58, 17 July 2019
Line 1:		Line 1:

	==Crystal Structure of Twin Arginine Translocase Receptor- TatC in DDM==		==Crystal Structure of Twin Arginine Translocase Receptor- TatC in DDM==
	<StructureSection load='4htt' size='340' side='right' caption='[[4htt]], [[Resolution\|resolution]] 6.80Å' scene=''>		<StructureSection load='4htt' size='340' side='right'caption='[[4htt]], [[Resolution\|resolution]] 6.80Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[4htt]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Bpt4 Bpt4]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4HTT OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4HTT FirstGlance]. <br>		<table><tr><td colspan='2'>[[4htt]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Bpt4 Bpt4]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4HTT OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4HTT FirstGlance]. <br>
Line 25:		Line 25:
	</StructureSection>		</StructureSection>
	[[Category: Bpt4]]		[[Category: Bpt4]]
			[[Category: Large Structures]]
	[[Category: Lysozyme]]		[[Category: Lysozyme]]
	[[Category: Clemons, W M]]		[[Category: Clemons, W M]]

OCA at 02:05, 5 August 2016

2016-08-05T02:05:52Z

← Older revision		Revision as of 02:05, 5 August 2016
Line 1:		Line 1:

	==Crystal Structure of Twin Arginine Translocase Receptor- TatC in DDM==		==Crystal Structure of Twin Arginine Translocase Receptor- TatC in DDM==
	<StructureSection load='4htt' size='340' side='right' caption='[[4htt]], [[Resolution\|resolution]] 6.80Å' scene=''>		<StructureSection load='4htt' size='340' side='right' caption='[[4htt]], [[Resolution\|resolution]] 6.80Å' scene=''>
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	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">tatC, aq_1267, E ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10665 BPT4])</td></tr>		<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">tatC, aq_1267, E ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10665 BPT4])</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Lysozyme Lysozyme], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.17 3.2.1.17] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Lysozyme Lysozyme], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.17 3.2.1.17] </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=4htt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4htt OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4htt RCSB], [http://www.ebi.ac.uk/pdbsum/4htt 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=4htt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4htt OCA], [http://pdbe.org/4htt PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4htt RCSB], [http://www.ebi.ac.uk/pdbsum/4htt PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4htt ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 18:		Line 19:
	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 4htt" style="background-color:#fffaf0;"></div>
	== References ==		== References ==
	<references/>		<references/>

OCA at 14:55, 25 December 2014

2014-12-25T14:55:50Z

← Older revision		Revision as of 14:55, 25 December 2014
Line 8:		Line 8:
	<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=4htt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4htt OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4htt RCSB], [http://www.ebi.ac.uk/pdbsum/4htt 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=4htt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4htt OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4htt RCSB], [http://www.ebi.ac.uk/pdbsum/4htt PDBsum]</span></td></tr>
	</table>		</table>
			== Function ==
			[[http://www.uniprot.org/uniprot/TATC_AQUAE TATC_AQUAE]] 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 (By similarity).
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==

OCA at 12:52, 21 December 2014

2014-12-21T12:52:09Z

← Older revision		Revision as of 12:52, 21 December 2014
Line 1:		Line 1:
	~~{{STRUCTURE_4htt\| PDB=4htt \| SCENE= }}~~		==Crystal Structure of Twin Arginine Translocase Receptor- TatC in DDM==
	===Crystal Structure of Twin Arginine Translocase Receptor- TatC in DDM===		<StructureSection load='4htt' size='340' side='right' caption='[[4htt]], [[Resolution\|resolution]] 6.80Å' scene=''>
	~~{{ABSTRACT_PUBMED_23583035}}~~		== Structural highlights ==
			<table><tr><td colspan='2'>[[4htt]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Bpt4 Bpt4]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4HTT OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4HTT FirstGlance]. <br>
			</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4hts\|4hts]]</td></tr>
			<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">tatC, aq_1267, E ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10665 BPT4])</td></tr>
			<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Lysozyme Lysozyme], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.17 3.2.1.17] </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=4htt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4htt OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4htt RCSB], [http://www.ebi.ac.uk/pdbsum/4htt PDBsum]</span></td></tr>
			</table>
			<div style="background-color:#fffaf0;">
			== Publication Abstract from PubMed ==
			In bacteria, two signal-sequence-dependent secretion pathways translocate proteins across the cytoplasmic membrane. Although the mechanism of the ubiquitous general secretory pathway is becoming well understood, that of the twin-arginine translocation pathway, responsible for translocation of folded proteins across the bilayer, is more mysterious. TatC, the largest and most conserved of three integral membrane components, provides the initial binding site of the signal sequence prior to pore assembly. Here, we present two crystal structures of TatC from the thermophilic bacteria Aquifex aeolicus at 4.0 A and 6.8 A resolution. The membrane architecture of TatC includes a glove-shaped structure with a lipid-exposed pocket predicted by molecular dynamics to distort the membrane. Correlating the biochemical literature to these results suggests that the signal sequence binds in this pocket, leading to structural changes that facilitate higher order assemblies.

	~~==Function==~~		The Glove-like Structure of the Conserved Membrane Protein TatC Provides Insight into Signal Sequence Recognition in Twin-Arginine Translocation.,Ramasamy S, Abrol R, Suloway CJ, Clemons WM Jr Structure. 2013 Apr 9. pii: S0969-2126(13)00085-3. doi:, 10.1016/j.str.2013.03.004. PMID:23583035<ref>PMID:23583035</ref>
	~~[[http://www~~.~~uniprot~~.~~org/uniprot/TATC_AQUAE TATC_AQUAE]] 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 (By similarity)~~.

	~~==About this Structure==~~		From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
	~~[[4htt]] is~~ a ~~2 chain structure~~. ~~Full crystallographic information is available from [http://oca~~.~~weizmann~~.~~ac.il~~/~~oca-bin/ocashort?id=4HTT OCA].~~		</div>
			== References ==
	==~~Reference~~==		<references/>
	~~<ref group="xtra">PMID:023583035</ref>~~<references ~~group="xtra"~~/><~~references~~/>		__TOC__
			</StructureSection>
			[[Category: Bpt4]]
	[[Category: Lysozyme]]		[[Category: Lysozyme]]
	[[Category: Clemons, W M.]]		[[Category: Clemons, W M]]
	[[Category: Ramasamy, S.]]		[[Category: Ramasamy, S]]
	[[Category: Suloway, C J.M.]]		[[Category: Suloway, C J.M]]
	[[Category: Hydrolase]]		[[Category: Hydrolase]]
	[[Category: Membrane]]		[[Category: Membrane]]
	[[Category: Twin arginine translocase receptor]]		[[Category: Twin arginine translocase receptor]]

OCA at 16:33, 19 June 2013

2013-06-19T16:33:28Z

← Older revision		Revision as of 16:33, 19 June 2013
Line 8:		Line 8:
	==About this Structure==		==About this Structure==
	[[4htt]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4HTT OCA].		[[4htt]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4HTT OCA].

			==Reference==
			<ref group="xtra">PMID:023583035</ref><references group="xtra"/><references/>
	[[Category: Lysozyme]]		[[Category: Lysozyme]]
	[[Category: Clemons, W M.]]		[[Category: Clemons, W M.]]

OCA at 07:40, 2 May 2013

2013-05-02T07:40:13Z

← Older revision		Revision as of 07:40, 2 May 2013
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	~~'''Unreleased structure'''~~		{{STRUCTURE_4htt\| PDB=4htt \| SCENE= }}
			===Crystal Structure of Twin Arginine Translocase Receptor- TatC in DDM===
			{{ABSTRACT_PUBMED_23583035}}

	~~The entry 4htt is ON HOLD until May 01 2014~~		==Function==
			[[http://www.uniprot.org/uniprot/TATC_AQUAE TATC_AQUAE]] 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 (By similarity).

	~~Authors~~: Ramasamy, S., Suloway, C.J.M.~~, Clemons Jr., W.M.~~		==About this Structure==
			[[4htt]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4HTT OCA].
	~~Description~~: ~~Crystal Structure of~~ Twin ~~Arginine Translocase Receptor-TatC in DDM~~		[[Category: Lysozyme]]
			[[Category: Clemons, W M.]]
			[[Category: Ramasamy, S.]]
			[[Category: Suloway, C J.M.]]
			[[Category: Hydrolase]]
			[[Category: Membrane]]
			[[Category: Twin arginine translocase receptor]]

OCA at 08:20, 16 January 2013

2013-01-16T08:20:26Z

← Older revision		Revision as of 08:20, 16 January 2013
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

	The entry 4htt is ON HOLD		The entry 4htt is ON HOLD until May 01 2014

	Authors: Ramasamy, S., Suloway, C.J.M., Clemons Jr., W.M.		Authors: Ramasamy, S., Suloway, C.J.M., Clemons Jr., W.M.

	Description: Crystal Structure of Twin Arginine Translocase Receptor-TatC in DDM		Description: Crystal Structure of Twin Arginine Translocase Receptor-TatC in DDM

OCA at 14:03, 28 November 2012

2012-11-28T14:03:48Z

← Older revision		Revision as of 14:03, 28 November 2012
Line 3:		Line 3:
	The entry 4htt is ON HOLD		The entry 4htt is ON HOLD

	Authors: Ramasamy, ~~Sureshkumar~~, Suloway, ~~Christian~~. J. M, Clemons Jr., ~~William~~. M		Authors: Ramasamy, S., Suloway, C.J.M., Clemons Jr., W.M.

	Description: Crystal Structure of Twin Arginine Translocase Receptor-~~TatC_T4Lysozyme fusion~~		Description: Crystal Structure of Twin Arginine Translocase Receptor-TatC in DDM