This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.

4cbw

From Proteopedia

(Difference between revisions)

Jump to: navigation, search

Revision as of 22:00, 5 August 2016

Crystal structure of Plasmodium berghei actin I with D-loop from muscle actin

Structural highlights

4cbw is a 2 chain structure with sequence from Lk3 transgenic mice and Plabe. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	, ,
Related:	4cbu, 4cbx
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[ACT1_PLABA] Actins are highly conserved proteins that are involved in various types of cell motility and are ubiquitously expressed in all eukaryotic cells. [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.

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^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ 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. Structural differences explain diverse functions of Plasmodium actins. PLoS Pathog. 2014 Apr 17;10(4):e1004091. doi: 10.1371/journal.ppat.1004091., eCollection 2014 Apr. PMID:24743229 doi:http://dx.doi.org/10.1371/journal.ppat.1004091

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 See Also
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/4cbw"

@@ Line 1: / Line 1: @@
 ==Crystal structure of Plasmodium berghei actin I with D-loop from muscle actin==
 <StructureSection load='4cbw' size='340' side='right' caption='[[4cbw]], [[Resolution|resolution]] 2.50&Aring;' 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>, <scene name='pdbligand=DIO:1,4-DIETHYLENE+DIOXIDE'>DIO</scene></td></tr>
 <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4cbu|4cbu]], [[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=4cbw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4cbw OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4cbw RCSB], [http://www.ebi.ac.uk/pdbsum/4cbw 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=4cbw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4cbw OCA], [http://pdbe.org/4cbw PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4cbw RCSB], [http://www.ebi.ac.uk/pdbsum/4cbw PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4cbw ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 17: / Line 18: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 4cbw" style="background-color:#fffaf0;"></div>
+==See Also==
+*[[Actin|Actin]]
+*[[Gelsolin|Gelsolin]]
 == References ==
 <references/>

4cbw

From Proteopedia

Revision as of 22:00, 5 August 2016

Crystal structure of Plasmodium berghei actin I with D-loop from muscle actin

Structural highlights

Function

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

Personal tools

Navigation

Search

Toolbox