4cbu - Revision history

OCA at 11:10, 9 May 2024

2024-05-09T11:10:58Z

←Older revision		Revision as of 11:10, 9 May 2024
Line 4:		Line 4:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[4cbu]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus] and [https://en.wikipedia.org/wiki/Plasmodium_falciparum Plasmodium falciparum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4CBU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4CBU FirstGlance]. <br>		<table><tr><td colspan='2'>[[4cbu]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus] and [https://en.wikipedia.org/wiki/Plasmodium_falciparum Plasmodium falciparum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4CBU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4CBU FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</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]] 1.3Å</td></tr>
		+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</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=4cbu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4cbu OCA], [https://pdbe.org/4cbu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4cbu RCSB], [https://www.ebi.ac.uk/pdbsum/4cbu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4cbu 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=4cbu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4cbu OCA], [https://pdbe.org/4cbu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4cbu RCSB], [https://www.ebi.ac.uk/pdbsum/4cbu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4cbu ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[https://www.uniprot.org/uniprot/ACT1_PLAFX ACT1_PLAFX]] Actins are highly conserved proteins that are involved in various types of cell motility and are ubiquitously expressed in all eukaryotic cells. Actin assembles into short polymer microfilaments, these are thought to contribute to parasite gliding motility.	+	[https://www.uniprot.org/uniprot/ACT1_PLAFX ACT1_PLAFX] Actins are highly conserved proteins that are involved in various types of cell motility and are ubiquitously expressed in all eukaryotic cells. Actin assembles into short polymer microfilaments, these are thought to contribute to parasite gliding motility.
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	Actins are highly conserved proteins and key players in central processes in all eukaryotic cells. The two actins of the malaria parasite are among the most divergent eukaryotic actins and also differ from each other more than isoforms in any other species. Microfilaments have not been directly observed in Plasmodium and are presumed to be short and highly dynamic. We show that actin I cannot complement actin II in male gametogenesis, suggesting critical structural differences. Cryo-EM reveals that Plasmodium actin I has a unique filament structure, whereas actin II filaments resemble canonical F-actin. Both Plasmodium actins hydrolyze ATP more efficiently than alpha-actin, and unlike any other actin, both parasite actins rapidly form short oligomers induced by ADP. Crystal structures of both isoforms pinpoint several structural changes in the monomers causing the unique polymerization properties. Inserting the canonical D-loop to Plasmodium actin I leads to the formation of long filaments in vitro. In vivo, this chimera restores gametogenesis in parasites lacking actin II, suggesting that stable filaments are required for exflagellation. Together, these data underline the divergence of eukaryotic actins and demonstrate how structural differences in the monomers translate into filaments with different properties, implying that even eukaryotic actins have faced different evolutionary pressures and followed different paths for developing their polymerization properties.
		+
		+	Structural differences explain diverse functions of Plasmodium actins.,Vahokoski J, Bhargav SP, Desfosses A, Andreadaki M, Kumpula EP, Martinez SM, Ignatev A, Lepper S, Frischknecht F, Siden-Kiamos I, Sachse C, Kursula I PLoS Pathog. 2014 Apr 17;10(4):e1004091. doi: 10.1371/journal.ppat.1004091., eCollection 2014 Apr. PMID:24743229<ref>PMID:24743229</ref>
		+
		+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
		+	</div>
		+	<div class="pdbe-citations 4cbu" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
	*[[Actin 3D structures\|Actin 3D structures]]		*[[Actin 3D structures\|Actin 3D structures]]
	*[[Gelsolin 3D structures\|Gelsolin 3D structures]]		*[[Gelsolin 3D structures\|Gelsolin 3D structures]]
		+	== References ==
		+	<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>

OCA at 17:37, 7 September 2022

2022-09-07T17:37:27Z

←Older revision		Revision as of 17:37, 7 September 2022
Line 3:		Line 3:
	<StructureSection load='4cbu' size='340' side='right'caption='[[4cbu]], [[Resolution\|resolution]] 1.30Å' scene=''>		<StructureSection load='4cbu' size='340' side='right'caption='[[4cbu]], [[Resolution\|resolution]] 1.30Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[4cbu]] is a 2 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/~~Lk3_transgenic_mice Lk3 transgenic mice~~] and [~~http~~://en.wikipedia.org/wiki/~~Plafa Plafa~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4CBU OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=4CBU FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[4cbu]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus] and [https://en.wikipedia.org/wiki/Plasmodium_falciparum Plasmodium falciparum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4CBU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4CBU FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>~~</td></tr>~~	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></td></tr>
-	~~<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4cbw\|4cbw]], [[4cbx\|4cbx]]~~</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=4cbu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4cbu OCA], [https://pdbe.org/4cbu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4cbu RCSB], [https://www.ebi.ac.uk/pdbsum/4cbu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4cbu 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=4cbu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4cbu OCA], [~~http~~://pdbe.org/4cbu PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=4cbu RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/4cbu PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=4cbu ProSAT]</span></td></tr>	+
	</table>		</table>
	== Function ==		== Function ==
-	[[~~http~~://www.uniprot.org/uniprot/ACT1_PLAFX ACT1_PLAFX]] Actins are highly conserved proteins that are involved in various types of cell motility and are ubiquitously expressed in all eukaryotic cells. Actin assembles into short polymer microfilaments, these are thought to contribute to parasite gliding motility. [[http://www.uniprot.org/uniprot/GELS_MOUSE GELS_MOUSE]] Calcium-regulated, actin-modulating protein that binds to the plus (or barbed) ends of actin monomers or filaments, preventing monomer exchange (end-blocking or capping). It can promote the assembly of monomers into filaments (nucleation) as well as sever filaments already formed. Plays a role in ciliogenesis.	+	[[https://www.uniprot.org/uniprot/ACT1_PLAFX ACT1_PLAFX]] Actins are highly conserved proteins that are involved in various types of cell motility and are ubiquitously expressed in all eukaryotic cells. Actin assembles into short polymer microfilaments, these are thought to contribute to parasite gliding motility.
-	~~<div style="background-color:#fffaf0;">~~	+
-	~~== Publication Abstract from PubMed ==~~	+
-	Actins are highly conserved proteins and key players in central processes in all eukaryotic cells. The two actins of the malaria parasite are among the most divergent eukaryotic actins and also differ from each other more than isoforms in any other species. Microfilaments have not been directly observed in Plasmodium and are presumed to be short and highly dynamic. We show that actin I cannot complement actin II in male gametogenesis, suggesting critical structural differences. Cryo-EM reveals that Plasmodium actin I has a unique filament structure, whereas actin II filaments resemble canonical F-actin. Both Plasmodium actins hydrolyze ATP more efficiently than alpha-actin, and unlike any other actin, both parasite actins rapidly form short oligomers induced by ADP. Crystal structures of both isoforms pinpoint several structural changes in the monomers causing the unique polymerization properties. Inserting the canonical D-loop to Plasmodium actin I leads to the formation of long filaments in vitro. In vivo, this chimera restores gametogenesis in parasites lacking actin II, suggesting that stable filaments are required for exflagellation. Together, these data underline the divergence of eukaryotic actins and demonstrate how structural differences in the monomers translate into filaments with different properties, implying that even eukaryotic actins have faced different evolutionary pressures and followed different paths for developing their polymerization properties.	+
-		+
-	Structural differences explain diverse functions of Plasmodium actins.,Vahokoski J, Bhargav SP, Desfosses A, Andreadaki M, Kumpula EP, Martinez SM, Ignatev A, Lepper S, Frischknecht F, Siden-Kiamos I, Sachse C, Kursula I PLoS Pathog. 2014 Apr 17;10(4):e1004091. doi: 10.1371/journal.ppat.1004091., eCollection 2014 Apr. PMID:24743229<ref>PMID:24743229</ref>	+
-		+
-	~~From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>~~	+
-	~~</div>~~	+
-	~~<div class="pdbe-citations 4cbu" style="background-color:#fffaf0;"></div>~~	+

	==See Also==		==See Also==
	*[[Actin 3D structures\|Actin 3D structures]]		*[[Actin 3D structures\|Actin 3D structures]]
-	*[[Gelsolin\|Gelsolin]]	+	*[[Gelsolin 3D structures\|Gelsolin 3D structures]]
-	~~== References ==~~	+
-	~~<references/>~~	+
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: ~~Lk3 transgenic mice~~]]	+	[[Category: Mus musculus]]
-	[[Category: ~~Plafa~~]]	+	[[Category: Plasmodium falciparum]]
-	[[Category: Andreadaki, M]]	+	[[Category: Andreadaki M]]
-	[[Category: Bhargav~~, S P~~]]	+	[[Category: Bhargav SP]]
-	[[Category: Desfosses, A]]	+	[[Category: Desfosses A]]
-	[[Category: Frischknecht, F]]	+	[[Category: Frischknecht F]]
-	[[Category: Ignatev, A]]	+	[[Category: Ignatev A]]
-	[[Category: Kumpula~~, E P~~]]	+	[[Category: Kumpula EP]]
-	[[Category: Kursula, I]]	+	[[Category: Kursula I]]
-	[[Category: Lepper, S]]	+	[[Category: Lepper S]]
-	[[Category: Martinez, S ~~Munico~~]]	+	[[Category: Munico Martinez S]]
-	[[Category: Sachse, C]]	+	[[Category: Sachse C]]
-	[[Category: Siden-Kiamos, I]]	+	[[Category: Siden-Kiamos I]]
-	[[Category: Vahokoski, J]]	+	[[Category: Vahokoski J]]
-	~~[[Category: Malaria]]~~	+
-	~~[[Category: Motility]]~~	+
-	~~[[Category: Motor protein]]~~	+
-	~~[[Category: Parasite~~]]	+

OCA at 08:50, 20 March 2019

2019-03-20T08:50:13Z

←Older revision		Revision as of 08:50, 20 March 2019
Line 1:		Line 1:

	==Crystal structure of Plasmodium falciparum actin I==		==Crystal structure of Plasmodium falciparum actin I==
-	<StructureSection load='4cbu' size='340' side='right' caption='[[4cbu]], [[Resolution\|resolution]] 1.30Å' scene=''>	+	<StructureSection load='4cbu' size='340' side='right'caption='[[4cbu]], [[Resolution\|resolution]] 1.30Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[4cbu]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Lk3_transgenic_mice Lk3 transgenic mice] and [http://en.wikipedia.org/wiki/Plafa Plafa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4CBU OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4CBU FirstGlance]. <br>		<table><tr><td colspan='2'>[[4cbu]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Lk3_transgenic_mice Lk3 transgenic mice] and [http://en.wikipedia.org/wiki/Plafa Plafa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4CBU OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4CBU FirstGlance]. <br>
Line 21:		Line 21:

	==See Also==		==See Also==
-	*[[Actin\|Actin]]	+	*[[Actin 3D structures\|Actin 3D structures]]
	*[[Gelsolin\|Gelsolin]]		*[[Gelsolin\|Gelsolin]]
	== References ==		== References ==
Line 27:		Line 27:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
		+	[[Category: Large Structures]]
	[[Category: Lk3 transgenic mice]]		[[Category: Lk3 transgenic mice]]
	[[Category: Plafa]]		[[Category: Plafa]]

OCA at 08:34, 4 August 2016

2016-08-04T08:34:53Z

←Older revision		Revision as of 08:34, 4 August 2016
Line 1:		Line 1:
		+
	==Crystal structure of Plasmodium falciparum actin I==		==Crystal structure of Plasmodium falciparum actin I==
	<StructureSection load='4cbu' size='340' side='right' caption='[[4cbu]], [[Resolution\|resolution]] 1.30Å' scene=''>		<StructureSection load='4cbu' size='340' side='right' caption='[[4cbu]], [[Resolution\|resolution]] 1.30Å' scene=''>
Line 5:		Line 6:
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4cbw\|4cbw]], [[4cbx\|4cbx]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4cbw\|4cbw]], [[4cbx\|4cbx]]</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=4cbu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4cbu OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4cbu RCSB], [http://www.ebi.ac.uk/pdbsum/4cbu 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=4cbu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4cbu OCA], [http://pdbe.org/4cbu PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4cbu RCSB], [http://www.ebi.ac.uk/pdbsum/4cbu PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4cbu ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 17:		Line 18:
	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 4cbu" style="background-color:#fffaf0;"></div>
		+
		+	==See Also==
		+	*[[Actin\|Actin]]
		+	*[[Gelsolin\|Gelsolin]]
	== References ==		== References ==
	<references/>		<references/>

OCA at 07:23, 25 December 2014

2014-12-25T07:23:10Z

←Older revision		Revision as of 07:23, 25 December 2014
Line 2:		Line 2:
	<StructureSection load='4cbu' size='340' side='right' caption='[[4cbu]], [[Resolution\|resolution]] 1.30Å' scene=''>		<StructureSection load='4cbu' size='340' side='right' caption='[[4cbu]], [[Resolution\|resolution]] 1.30Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[4cbu]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4CBU OCA]. <br>	+	<table><tr><td colspan='2'>[[4cbu]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Lk3_transgenic_mice Lk3 transgenic mice] and [http://en.wikipedia.org/wiki/Plafa Plafa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4CBU OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4CBU FirstGlance]. <br>
-	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene><br>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></td></tr>
-	<tr><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4cbw\|4cbw]], [[4cbx\|4cbx]]</td></tr>	+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4cbw\|4cbw]], [[4cbx\|4cbx]]</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>~~	+	<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=4cbu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4cbu OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4cbu RCSB], [http://www.ebi.ac.uk/pdbsum/4cbu PDBsum]</span></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=4cbu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4cbu OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4cbu RCSB], [http://www.ebi.ac.uk/pdbsum/4cbu PDBsum]</span></td></tr>	+	</table>
-	<table>	+	== Function ==
		+	[[http://www.uniprot.org/uniprot/ACT1_PLAFX ACT1_PLAFX]] Actins are highly conserved proteins that are involved in various types of cell motility and are ubiquitously expressed in all eukaryotic cells. Actin assembles into short polymer microfilaments, these are thought to contribute to parasite gliding motility. [[http://www.uniprot.org/uniprot/GELS_MOUSE GELS_MOUSE]] Calcium-regulated, actin-modulating protein that binds to the plus (or barbed) ends of actin monomers or filaments, preventing monomer exchange (end-blocking or capping). It can promote the assembly of monomers into filaments (nucleation) as well as sever filaments already formed. Plays a role in ciliogenesis.
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 14:		Line 15:
	Structural differences explain diverse functions of Plasmodium actins.,Vahokoski J, Bhargav SP, Desfosses A, Andreadaki M, Kumpula EP, Martinez SM, Ignatev A, Lepper S, Frischknecht F, Siden-Kiamos I, Sachse C, Kursula I PLoS Pathog. 2014 Apr 17;10(4):e1004091. doi: 10.1371/journal.ppat.1004091., eCollection 2014 Apr. PMID:24743229<ref>PMID:24743229</ref>		Structural differences explain diverse functions of Plasmodium actins.,Vahokoski J, Bhargav SP, Desfosses A, Andreadaki M, Kumpula EP, Martinez SM, Ignatev A, Lepper S, Frischknecht F, Siden-Kiamos I, Sachse C, Kursula I PLoS Pathog. 2014 Apr 17;10(4):e1004091. doi: 10.1371/journal.ppat.1004091., eCollection 2014 Apr. PMID:24743229<ref>PMID:24743229</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 20:		Line 21:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: Andreadaki, M.]]	+	[[Category: Lk3 transgenic mice]]
-	[[Category: Bhargav, S P.]]	+	[[Category: Plafa]]
-	[[Category: Desfosses, A.]]	+	[[Category: Andreadaki, M]]
-	[[Category: Frischknecht, F.]]	+	[[Category: Bhargav, S P]]
-	[[Category: Ignatev, A.]]	+	[[Category: Desfosses, A]]
-	[[Category: Kumpula, E P.]]	+	[[Category: Frischknecht, F]]
-	[[Category: Kursula, I.]]	+	[[Category: Ignatev, A]]
-	[[Category: Lepper, S.]]	+	[[Category: Kumpula, E P]]
-	[[Category: Martinez, S Munico.]]	+	[[Category: Kursula, I]]
-	[[Category: Sachse, C.]]	+	[[Category: Lepper, S]]
-	[[Category: Siden-Kiamos, I.]]	+	[[Category: Martinez, S Munico]]
-	[[Category: Vahokoski, J.]]	+	[[Category: Sachse, C]]
		+	[[Category: Siden-Kiamos, I]]
		+	[[Category: Vahokoski, J]]
	[[Category: Malaria]]		[[Category: Malaria]]
	[[Category: Motility]]		[[Category: Motility]]
	[[Category: Motor protein]]		[[Category: Motor protein]]
	[[Category: Parasite]]		[[Category: Parasite]]

OCA at 09:23, 1 May 2014

2014-05-01T09:23:42Z

←Older revision		Revision as of 09:23, 1 May 2014
Line 15:		Line 15:

	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 09:19, 1 May 2014

2014-05-01T09:19:47Z

←Older revision		Revision as of 09:19, 1 May 2014
Line 2:		Line 2:
	<StructureSection load='4cbu' size='340' side='right' caption='[[4cbu]], [[Resolution\|resolution]] 1.30Å' scene=''>		<StructureSection load='4cbu' size='340' side='right' caption='[[4cbu]], [[Resolution\|resolution]] 1.30Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	[[4cbu]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4CBU OCA]. <br>	+	<table><tr><td colspan='2'>[[4cbu]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4CBU OCA]. <br>
-	<b>[[Ligand\|Ligands:]]</b> <scene name='pdbligand=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene><br>	+	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene><br>
-	<b>[[Related_structure\|Related:]]</b> [[4cbw\|4cbw]], [[4cbx\|4cbx]]<br>	+	<tr><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4cbw\|4cbw]], [[4cbx\|4cbx]]</td></tr>
-	<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>	+	<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=4cbu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4cbu OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4cbu RCSB], [http://www.ebi.ac.uk/pdbsum/4cbu 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=4cbu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4cbu OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4cbu RCSB], [http://www.ebi.ac.uk/pdbsum/4cbu PDBsum]</span></td></tr>
		+	<table>
		+	<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
	Actins are highly conserved proteins and key players in central processes in all eukaryotic cells. The two actins of the malaria parasite are among the most divergent eukaryotic actins and also differ from each other more than isoforms in any other species. Microfilaments have not been directly observed in Plasmodium and are presumed to be short and highly dynamic. We show that actin I cannot complement actin II in male gametogenesis, suggesting critical structural differences. Cryo-EM reveals that Plasmodium actin I has a unique filament structure, whereas actin II filaments resemble canonical F-actin. Both Plasmodium actins hydrolyze ATP more efficiently than alpha-actin, and unlike any other actin, both parasite actins rapidly form short oligomers induced by ADP. Crystal structures of both isoforms pinpoint several structural changes in the monomers causing the unique polymerization properties. Inserting the canonical D-loop to Plasmodium actin I leads to the formation of long filaments in vitro. In vivo, this chimera restores gametogenesis in parasites lacking actin II, suggesting that stable filaments are required for exflagellation. Together, these data underline the divergence of eukaryotic actins and demonstrate how structural differences in the monomers translate into filaments with different properties, implying that even eukaryotic actins have faced different evolutionary pressures and followed different paths for developing their polymerization properties.		Actins are highly conserved proteins and key players in central processes in all eukaryotic cells. The two actins of the malaria parasite are among the most divergent eukaryotic actins and also differ from each other more than isoforms in any other species. Microfilaments have not been directly observed in Plasmodium and are presumed to be short and highly dynamic. We show that actin I cannot complement actin II in male gametogenesis, suggesting critical structural differences. Cryo-EM reveals that Plasmodium actin I has a unique filament structure, whereas actin II filaments resemble canonical F-actin. Both Plasmodium actins hydrolyze ATP more efficiently than alpha-actin, and unlike any other actin, both parasite actins rapidly form short oligomers induced by ADP. Crystal structures of both isoforms pinpoint several structural changes in the monomers causing the unique polymerization properties. Inserting the canonical D-loop to Plasmodium actin I leads to the formation of long filaments in vitro. In vivo, this chimera restores gametogenesis in parasites lacking actin II, suggesting that stable filaments are required for exflagellation. Together, these data underline the divergence of eukaryotic actins and demonstrate how structural differences in the monomers translate into filaments with different properties, implying that even eukaryotic actins have faced different evolutionary pressures and followed different paths for developing their polymerization properties.
Line 13:		Line 15:

	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__

OCA at 09:52, 30 April 2014

2014-04-30T09:52:07Z

←Older revision		Revision as of 09:52, 30 April 2014
Line 3:		Line 3:
	== Structural highlights ==		== Structural highlights ==
	[[4cbu]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4CBU OCA]. <br>		[[4cbu]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4CBU OCA]. <br>
-	<b>Related:</b> [[4cbw\|4cbw]], [[4cbx\|4cbx]]<br>	+	<b>[[Ligand\|Ligands:]]</b> <scene name='pdbligand=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene><br>
		+	<b>[[Related_structure\|Related:]]</b> [[4cbw\|4cbw]], [[4cbx\|4cbx]]<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>		<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>
		+	<b>Resources:</b> <span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4cbu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4cbu OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4cbu RCSB], [http://www.ebi.ac.uk/pdbsum/4cbu PDBsum]</span><br>
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
	Actins are highly conserved proteins and key players in central processes in all eukaryotic cells. The two actins of the malaria parasite are among the most divergent eukaryotic actins and also differ from each other more than isoforms in any other species. Microfilaments have not been directly observed in Plasmodium and are presumed to be short and highly dynamic. We show that actin I cannot complement actin II in male gametogenesis, suggesting critical structural differences. Cryo-EM reveals that Plasmodium actin I has a unique filament structure, whereas actin II filaments resemble canonical F-actin. Both Plasmodium actins hydrolyze ATP more efficiently than alpha-actin, and unlike any other actin, both parasite actins rapidly form short oligomers induced by ADP. Crystal structures of both isoforms pinpoint several structural changes in the monomers causing the unique polymerization properties. Inserting the canonical D-loop to Plasmodium actin I leads to the formation of long filaments in vitro. In vivo, this chimera restores gametogenesis in parasites lacking actin II, suggesting that stable filaments are required for exflagellation. Together, these data underline the divergence of eukaryotic actins and demonstrate how structural differences in the monomers translate into filaments with different properties, implying that even eukaryotic actins have faced different evolutionary pressures and followed different paths for developing their polymerization properties.		Actins are highly conserved proteins and key players in central processes in all eukaryotic cells. The two actins of the malaria parasite are among the most divergent eukaryotic actins and also differ from each other more than isoforms in any other species. Microfilaments have not been directly observed in Plasmodium and are presumed to be short and highly dynamic. We show that actin I cannot complement actin II in male gametogenesis, suggesting critical structural differences. Cryo-EM reveals that Plasmodium actin I has a unique filament structure, whereas actin II filaments resemble canonical F-actin. Both Plasmodium actins hydrolyze ATP more efficiently than alpha-actin, and unlike any other actin, both parasite actins rapidly form short oligomers induced by ADP. Crystal structures of both isoforms pinpoint several structural changes in the monomers causing the unique polymerization properties. Inserting the canonical D-loop to Plasmodium actin I leads to the formation of long filaments in vitro. In vivo, this chimera restores gametogenesis in parasites lacking actin II, suggesting that stable filaments are required for exflagellation. Together, these data underline the divergence of eukaryotic actins and demonstrate how structural differences in the monomers translate into filaments with different properties, implying that even eukaryotic actins have faced different evolutionary pressures and followed different paths for developing their polymerization properties.

OCA at 07:51, 30 April 2014

2014-04-30T07:51:25Z

←Older revision		Revision as of 07:51, 30 April 2014
Line 1:		Line 1:
-	'''~~Unreleased structure~~'''	+	==Crystal structure of Plasmodium falciparum actin I==
		+	<StructureSection load='4cbu' size='340' side='right' caption='[[4cbu]], [[Resolution\|resolution]] 1.30Å' scene=''>
		+	== Structural highlights ==
		+	[[4cbu]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4CBU OCA]. <br>
		+	<b>Related:</b> [[4cbw\|4cbw]], [[4cbx\|4cbx]]<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>
		+	== Publication Abstract from PubMed ==
		+	Actins are highly conserved proteins and key players in central processes in all eukaryotic cells. The two actins of the malaria parasite are among the most divergent eukaryotic actins and also differ from each other more than isoforms in any other species. Microfilaments have not been directly observed in Plasmodium and are presumed to be short and highly dynamic. We show that actin I cannot complement actin II in male gametogenesis, suggesting critical structural differences. Cryo-EM reveals that Plasmodium actin I has a unique filament structure, whereas actin II filaments resemble canonical F-actin. Both Plasmodium actins hydrolyze ATP more efficiently than alpha-actin, and unlike any other actin, both parasite actins rapidly form short oligomers induced by ADP. Crystal structures of both isoforms pinpoint several structural changes in the monomers causing the unique polymerization properties. Inserting the canonical D-loop to Plasmodium actin I leads to the formation of long filaments in vitro. In vivo, this chimera restores gametogenesis in parasites lacking actin II, suggesting that stable filaments are required for exflagellation. Together, these data underline the divergence of eukaryotic actins and demonstrate how structural differences in the monomers translate into filaments with different properties, implying that even eukaryotic actins have faced different evolutionary pressures and followed different paths for developing their polymerization properties.

-	~~The entry 4cbu is ON HOLD until Paper Publication~~	+	Structural differences explain diverse functions of Plasmodium actins.,Vahokoski J, Bhargav SP, Desfosses A, Andreadaki M, Kumpula EP, Martinez SM, Ignatev A, Lepper S, Frischknecht F, Siden-Kiamos I, Sachse C, Kursula I PLoS Pathog. 2014 Apr 17;10(4):e1004091. doi: 10.1371/journal.ppat.1004091., eCollection 2014 Apr. PMID:24743229<ref>PMID:24743229</ref>

-	~~Authors: Vahokoski~~, J., Bhargav, S.P., Desfosses, A., ~~Andreadaki, M~~., Kumpula, E.P., ~~Ignatev, A~~.~~, Munico Martinez~~, S.~~, Lepper~~, S., ~~Frischknecht, F~~., Siden-Kiamos, I., ~~Sachse, C., Kursula, I~~.	+	From MEDLINEÂ®/PubMedÂ®, a database of the U.S. National Library of Medicine.<br>
-		+	== References ==
-	~~Description~~: ~~Crystal structure of Plasmodium falciparum actin I~~	+	<references/>
		+	__TOC__
		+	</StructureSection>
		+	[[Category: Andreadaki, M.]]
		+	[[Category: Bhargav, S P.]]
		+	[[Category: Desfosses, A.]]
		+	[[Category: Frischknecht, F.]]
		+	[[Category: Ignatev, A.]]
		+	[[Category: Kumpula, E P.]]
		+	[[Category: Kursula, I.]]
		+	[[Category: Lepper, S.]]
		+	[[Category: Martinez, S Munico.]]
		+	[[Category: Sachse, C.]]
		+	[[Category: Siden-Kiamos, I.]]
		+	[[Category: Vahokoski, J.]]
		+	[[Category: Malaria]]
		+	[[Category: Motility]]
		+	[[Category: Motor protein]]
		+	[[Category: Parasite]]

OCA at 08:10, 2 April 2014

2014-04-02T08:10:30Z

←Older revision		Revision as of 08:10, 2 April 2014
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

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

	Authors: Vahokoski, J., Bhargav, S.P., Desfosses, A., Andreadaki, M., Kumpula, E.P., Ignatev, A., Munico Martinez, S., Lepper, S., Frischknecht, F., Siden-Kiamos, I., Sachse, C., Kursula, I.		Authors: Vahokoski, J., Bhargav, S.P., Desfosses, A., Andreadaki, M., Kumpula, E.P., Ignatev, A., Munico Martinez, S., Lepper, S., Frischknecht, F., Siden-Kiamos, I., Sachse, C., Kursula, I.

	Description: Crystal structure of Plasmodium falciparum actin I		Description: Crystal structure of Plasmodium falciparum actin I