4o32 - Revision history

OCA at 14:07, 13 March 2024

OCA — Wed, 13 Mar 2024 14:07:35 GMT

←Older revision		Revision as of 14:07, 13 March 2024
Line 10:		Line 10:
	== Function ==		== Function ==
	[https://www.uniprot.org/uniprot/THIO2_PLAF7 THIO2_PLAF7] Participates in various redox reactions through the reversible oxidation of its active center dithiol to a disulfide and catalyzes dithiol-disulfide exchange reactions (PubMed:16910770, PubMed:22355694). As part of the translocon PTEX complex, plays a role in the export of parasite proteins into the host erythrocyte (By similarity). The translocon PTEX complex is a multi-protein machinery resident in the parasite parasitophorous vacuolar membrane, responsible for protein secretion into host cells (PubMed:19536257). May contribute to the unfolding of proteins containing the PEXEL localization motif before their passage through the translocon or regulate the PTEX complex function (PubMed:19536257).[UniProtKB:A0A509AQW5]<ref>PMID:16910770</ref> <ref>PMID:19536257</ref> <ref>PMID:22355694</ref> <ref>PMID:19536257</ref>		[https://www.uniprot.org/uniprot/THIO2_PLAF7 THIO2_PLAF7] Participates in various redox reactions through the reversible oxidation of its active center dithiol to a disulfide and catalyzes dithiol-disulfide exchange reactions (PubMed:16910770, PubMed:22355694). As part of the translocon PTEX complex, plays a role in the export of parasite proteins into the host erythrocyte (By similarity). The translocon PTEX complex is a multi-protein machinery resident in the parasite parasitophorous vacuolar membrane, responsible for protein secretion into host cells (PubMed:19536257). May contribute to the unfolding of proteins containing the PEXEL localization motif before their passage through the translocon or regulate the PTEX complex function (PubMed:19536257).[UniProtKB:A0A509AQW5]<ref>PMID:16910770</ref> <ref>PMID:19536257</ref> <ref>PMID:22355694</ref> <ref>PMID:19536257</ref>
-	<div style="background-color:#fffaf0;">
-	== Publication Abstract from PubMed ==
-	Survival of the malaria parasite Plasmodium falciparum when it infects red blood cells depends upon its ability to export hundreds of its proteins beyond an encasing vacuole. Protein export is mediated by a parasite-derived protein complex, the Plasmodium translocon of exported proteins (PTEX), and requires unfolding of the different cargos prior to their translocation across the vacuolar membrane. Unfolding is performed by the AAA+protein unfoldase HSP101/ClpB2 and the thioredoxin-2 enzyme (TRX2). Protein trafficking is dramatically impaired in parasites with defective HSP101 or lacking TRX2. These two PTEX subunits drive export and are targets for the design of a novel class of antimalarials: protein export inhibitors. To rationalize inhibitor design, we solved the crystal structure of Pfal-TRX2 at 2.2-A resolution. Within the asymmetric unit, the three different copies of this protein disulfide reductase sample its two redox catalytic states. Size exclusion chromatography and small-angle X-ray scattering (SAXS) analyses demonstrate that Pfal-TRX2 is monomeric in solution. A non-conserved N-terminal extension precedes the canonical thioredoxin-fold; although it is not observed in our structure, our solution analysis suggests it is flexible in contrast to Plasmodium thioredoxin-1. This represents a first step towards the reconstitution of the entire PTEX for mechanistic and structural studies.
-
-	Crystal structure and solution characterization of the thioredoxin-2 from Plasmodium falciparum, a constituent of an essential parasitic protein export complex.,Peng M, Cascio D, Egea PF Biochem Biophys Res Commun. 2014 Dec 2. pii: S0006-291X(14)02137-8. doi:, 10.1016/j.bbrc.2014.11.096. PMID:25475729<ref>PMID:25475729</ref>
-
-	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	</div>
-	<div class="pdbe-citations 4o32" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==

OCA at 17:06, 20 September 2023

OCA — Wed, 20 Sep 2023 17:06:24 GMT

←Older revision		Revision as of 17:06, 20 September 2023
Line 4:		Line 4:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[4o32]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Plasmodium_falciparum_3D7 Plasmodium falciparum 3D7]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4O32 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4O32 FirstGlance]. <br>		<table><tr><td colspan='2'>[[4o32]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Plasmodium_falciparum_3D7 Plasmodium falciparum 3D7]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4O32 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4O32 FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene></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]] 2.196Å</td></tr>
		+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene></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=4o32 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4o32 OCA], [https://pdbe.org/4o32 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4o32 RCSB], [https://www.ebi.ac.uk/pdbsum/4o32 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4o32 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=4o32 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4o32 OCA], [https://pdbe.org/4o32 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4o32 RCSB], [https://www.ebi.ac.uk/pdbsum/4o32 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4o32 ProSAT]</span></td></tr>
	</table>		</table>

OCA at 08:54, 18 January 2023

OCA — Wed, 18 Jan 2023 08:54:02 GMT

←Older revision		Revision as of 08:54, 18 January 2023
Line 1:		Line 1:

	==Structure of a malarial protein==		==Structure of a malarial protein==
-	<StructureSection load='4o32' size='340' side='right' caption='[[4o32]], [[Resolution\|resolution]] 2.20Å' scene=''>	+	<StructureSection load='4o32' size='340' side='right'caption='[[4o32]], [[Resolution\|resolution]] 2.20Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[4o32]] is a 3 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/~~Plaf7 Plaf7~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4O32 OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=4O32 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[4o32]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Plasmodium_falciparum_3D7 Plasmodium falciparum 3D7]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4O32 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4O32 FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>~~</td></tr>~~	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene></td></tr>
-	~~<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4irf\|4irf]], [[4iod\|4iod]], [[3ul3\|3ul3]]</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=4o32 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4o32 OCA], [https://pdbe.org/4o32 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4o32 RCSB], [https://www.ebi.ac.uk/pdbsum/4o32 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4o32 ProSAT]</span></td></tr>
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">MAL13P1.225, PF3D7_1345100, trx2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=36329 PLAF7]), PF3D7_1345100 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=36329 PLAF7])</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=4o32 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4o32 OCA], [~~http~~://pdbe.org/4o32 PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=4o32 RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/4o32 PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=4o32 ProSAT]</span></td></tr>	+
	</table>		</table>
		+	== Function ==
		+	[https://www.uniprot.org/uniprot/THIO2_PLAF7 THIO2_PLAF7] Participates in various redox reactions through the reversible oxidation of its active center dithiol to a disulfide and catalyzes dithiol-disulfide exchange reactions (PubMed:16910770, PubMed:22355694). As part of the translocon PTEX complex, plays a role in the export of parasite proteins into the host erythrocyte (By similarity). The translocon PTEX complex is a multi-protein machinery resident in the parasite parasitophorous vacuolar membrane, responsible for protein secretion into host cells (PubMed:19536257). May contribute to the unfolding of proteins containing the PEXEL localization motif before their passage through the translocon or regulate the PTEX complex function (PubMed:19536257).[UniProtKB:A0A509AQW5]<ref>PMID:16910770</ref> <ref>PMID:19536257</ref> <ref>PMID:22355694</ref> <ref>PMID:19536257</ref>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 18:		Line 18:
	</div>		</div>
	<div class="pdbe-citations 4o32" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 4o32" style="background-color:#fffaf0;"></div>
		+
		+	==See Also==
		+	*[[Thioredoxin 3D structures\|Thioredoxin 3D structures]]
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Plaf7~~]]	+	[[Category: Large Structures]]
-	[[Category: Cascio, D]]	+	[[Category: Plasmodium falciparum 3D7]]
-	[[Category: Egea~~, P F~~]]	+	[[Category: Cascio D]]
-	[[Category: Koehl, A]]	+	[[Category: Egea PF]]
-	[[Category: Peng, M]]	+	[[Category: Koehl A]]
-	~~[[Category: Malaria]]~~	+	[[Category: Peng M]]
-	~~[[Category: Oxidoreductase]]~~	+
-	~~[[Category: Parasitophorous vacuole of malarial parasite]]~~	+
-	~~[[Category: Protein export]]~~	+
-	~~[[Category: Protein-disulfide-reductase~~]]	+

OCA at 08:20, 22 November 2017

OCA — Wed, 22 Nov 2017 08:20:30 GMT

←Older revision		Revision as of 08:20, 22 November 2017
Line 3:		Line 3:
	<StructureSection load='4o32' size='340' side='right' caption='[[4o32]], [[Resolution\|resolution]] 2.20Å' scene=''>		<StructureSection load='4o32' size='340' side='right' caption='[[4o32]], [[Resolution\|resolution]] 2.20Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[4o32]] is a 3 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4O32 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4O32 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[4o32]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Plaf7 Plaf7]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4O32 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4O32 FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4irf\|4irf]], [[4iod\|4iod]], [[3ul3\|3ul3]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4irf\|4irf]], [[4iod\|4iod]], [[3ul3\|3ul3]]</td></tr>
		+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">MAL13P1.225, PF3D7_1345100, trx2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=36329 PLAF7]), PF3D7_1345100 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=36329 PLAF7])</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=4o32 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4o32 OCA], [http://pdbe.org/4o32 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4o32 RCSB], [http://www.ebi.ac.uk/pdbsum/4o32 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4o32 ProSAT]</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=4o32 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4o32 OCA], [http://pdbe.org/4o32 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4o32 RCSB], [http://www.ebi.ac.uk/pdbsum/4o32 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4o32 ProSAT]</span></td></tr>
	</table>		</table>
Line 17:		Line 18:
	</div>		</div>
	<div class="pdbe-citations 4o32" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 4o32" style="background-color:#fffaf0;"></div>
-
-	==See Also==
-	*[[Thioredoxin\|Thioredoxin]]
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
		+	[[Category: Plaf7]]
	[[Category: Cascio, D]]		[[Category: Cascio, D]]
	[[Category: Egea, P F]]		[[Category: Egea, P F]]

OCA at 07:48, 11 August 2016

OCA — Thu, 11 Aug 2016 07:48:21 GMT

←Older revision		Revision as of 07:48, 11 August 2016
Line 1:		Line 1:
		+
	==Structure of a malarial protein==		==Structure of a malarial protein==
	<StructureSection load='4o32' size='340' side='right' caption='[[4o32]], [[Resolution\|resolution]] 2.20Å' scene=''>		<StructureSection load='4o32' size='340' side='right' caption='[[4o32]], [[Resolution\|resolution]] 2.20Å' scene=''>
Line 5:		Line 6:
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4irf\|4irf]], [[4iod\|4iod]], [[3ul3\|3ul3]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4irf\|4irf]], [[4iod\|4iod]], [[3ul3\|3ul3]]</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=4o32 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4o32 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4o32 RCSB], [http://www.ebi.ac.uk/pdbsum/4o32 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=4o32 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4o32 OCA], [http://pdbe.org/4o32 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4o32 RCSB], [http://www.ebi.ac.uk/pdbsum/4o32 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4o32 ProSAT]</span></td></tr>
	</table>		</table>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
Line 15:		Line 16:
	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 4o32" style="background-color:#fffaf0;"></div>
		+
		+	==See Also==
		+	*[[Thioredoxin\|Thioredoxin]]
	== References ==		== References ==
	<references/>		<references/>

OCA at 10:55, 24 December 2014

OCA — Wed, 24 Dec 2014 10:55:55 GMT

←Older revision		Revision as of 10:55, 24 December 2014
Line 1:		Line 1:
-	'''~~Unreleased~~ structure'''	+	==Structure of a malarial protein==
		+	<StructureSection load='4o32' size='340' side='right' caption='[[4o32]], [[Resolution\|resolution]] 2.20Å' scene=''>
		+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[4o32]] is a 3 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4O32 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4O32 FirstGlance]. <br>
		+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene></td></tr>
		+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4irf\|4irf]], [[4iod\|4iod]], [[3ul3\|3ul3]]</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=4o32 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4o32 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4o32 RCSB], [http://www.ebi.ac.uk/pdbsum/4o32 PDBsum]</span></td></tr>
		+	</table>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	Survival of the malaria parasite Plasmodium falciparum when it infects red blood cells depends upon its ability to export hundreds of its proteins beyond an encasing vacuole. Protein export is mediated by a parasite-derived protein complex, the Plasmodium translocon of exported proteins (PTEX), and requires unfolding of the different cargos prior to their translocation across the vacuolar membrane. Unfolding is performed by the AAA+protein unfoldase HSP101/ClpB2 and the thioredoxin-2 enzyme (TRX2). Protein trafficking is dramatically impaired in parasites with defective HSP101 or lacking TRX2. These two PTEX subunits drive export and are targets for the design of a novel class of antimalarials: protein export inhibitors. To rationalize inhibitor design, we solved the crystal structure of Pfal-TRX2 at 2.2-A resolution. Within the asymmetric unit, the three different copies of this protein disulfide reductase sample its two redox catalytic states. Size exclusion chromatography and small-angle X-ray scattering (SAXS) analyses demonstrate that Pfal-TRX2 is monomeric in solution. A non-conserved N-terminal extension precedes the canonical thioredoxin-fold; although it is not observed in our structure, our solution analysis suggests it is flexible in contrast to Plasmodium thioredoxin-1. This represents a first step towards the reconstitution of the entire PTEX for mechanistic and structural studies.

-	~~The entry 4o32 is ON HOLD until Paper Publication~~	+	Crystal structure and solution characterization of the thioredoxin-2 from Plasmodium falciparum, a constituent of an essential parasitic protein export complex.,Peng M, Cascio D, Egea PF Biochem Biophys Res Commun. 2014 Dec 2. pii: S0006-291X(14)02137-8. doi:, 10.1016/j.bbrc.2014.11.096. PMID:25475729<ref>PMID:25475729</ref>

-	~~Authors~~: Egea, P.F., Koehl, A., Peng, M~~., Cascio, D.~~	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-		+	</div>
-	~~Description~~: ~~Structure~~ of a malarial ~~protein~~	+	== References ==
		+	<references/>
		+	__TOC__
		+	</StructureSection>
		+	[[Category: Cascio, D]]
		+	[[Category: Egea, P F]]
		+	[[Category: Koehl, A]]
		+	[[Category: Peng, M]]
		+	[[Category: Malaria]]
		+	[[Category: Oxidoreductase]]
		+	[[Category: Parasitophorous vacuole of malarial parasite]]
		+	[[Category: Protein export]]
		+	[[Category: Protein-disulfide-reductase]]

OCA at 16:10, 19 February 2014

OCA — Wed, 19 Feb 2014 16:10:27 GMT

←Older revision		Revision as of 16:10, 19 February 2014
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

-	The entry 4o32 is ON HOLD	+	The entry 4o32 is ON HOLD until Paper Publication

	Authors: Egea, P.F., Koehl, A., Peng, M., Cascio, D.		Authors: Egea, P.F., Koehl, A., Peng, M., Cascio, D.

	Description: Structure of a malarial protein		Description: Structure of a malarial protein

OCA: Protected "4o32" [edit=sysop:move=sysop]

OCA — Wed, 25 Dec 2013 09:32:05 GMT

Protected "4o32" [edit=sysop:move=sysop]

←Older revision

Revision as of 09:32, 25 December 2013

OCA: New page: '''Unreleased structure''' The entry 4o32 is ON HOLD Authors: Egea, P.F., Koehl, A., Peng, M., Cascio, D. Description: Structure of a malarial protein

OCA — Wed, 25 Dec 2013 09:32:04 GMT

New page: '''Unreleased structure''' The entry 4o32 is ON HOLD Authors: Egea, P.F., Koehl, A., Peng, M., Cascio, D. Description: Structure of a malarial protein

New page

'''Unreleased structure'''

The entry 4o32 is ON HOLD

Authors: Egea, P.F., Koehl, A., Peng, M., Cascio, D.

Description: Structure of a malarial protein