4efh

From Proteopedia

(Difference between revisions)

Revision as of 20:39, 5 August 2016

Acanthamoeba Actin complex with Spir domain D

Structural highlights

4efh is a 2 chain structure with sequence from Acanthamoeba castellanii and Drome. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	,
Related:	3ue5
Gene:	spir, p150-Spir, CG10076 (DROME)
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[ACT1_ACACA] Actins are highly conserved proteins that are involved in various types of cell motility and are ubiquitously expressed in all eukaryotic cells. [SPIR_DROME] Acts as an actin nucleation factor, remains associated with the slow-growing pointed end of the new filament. Promotes dissociation of capu from the barbed end of actin filaments. Involved in intracellular vesicle transport along actin fibers, providing a novel link between actin cytoskeleton dynamics and intracellular transport. Required for localization of determinants within the developing oocyte to the posterior pole and to the dorsal anterior corner. Links Rho family signaling and Jnk function to the actin cytoskeleton.^[1] ^[2] ^[3] ^[4] ^[5]

Publication Abstract from PubMed

Spire is a WH2 domain-containing actin nucleator essential for establishing an actin mesh during oogenesis. In vitro, in addition to nucleating filaments, Spire can sever them and sequester actin monomers. Understanding how Spire is capable of these disparate functions and which are physiologically relevant is an important goal. To study severing, we examined the effect of Drosophila Spire on preformed filaments in bulk and single filament assays. We observed rapid depolymerization of actin filaments by Spire, which we conclude is largely due to its sequestration activity and enhanced by its weak severing activity. We also studied the solution and crystal structures of Spire-actin complexes. We find structural and functional differences between constructs containing four WH2-domains (Spir-ABCD) and two WH2-domains (Spir-CD) that may provide insight into mechanisms of nucleation and sequestration. Intriguingly, we observed lateral interactions between actin monomers associated with Spir-ABCD, suggesting that the structures built by these four tandem WH2 domains are more complex than originally imagined. Finally, we propose that Spire-actin mixtures contain both nuclei and sequestration structures.

Multiple forms of Spire-actin complexes and their functional consequences.,Chen CK, Sawaya MR, Phillips ML, Reisler E, Quinlan ME J Biol Chem. 2012 Feb 8. PMID:22334675^[6]

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

References

↑ Wellington A, Emmons S, James B, Calley J, Grover M, Tolias P, Manseau L. Spire contains actin binding domains and is related to ascidian posterior end mark-5. Development. 1999 Dec;126(23):5267-74. PMID:10556052
↑ Otto IM, Raabe T, Rennefahrt UE, Bork P, Rapp UR, Kerkhoff E. The p150-Spir protein provides a link between c-Jun N-terminal kinase function and actin reorganization. Curr Biol. 2000 Mar 23;10(6):345-8. PMID:10744979
↑ Quinlan ME, Heuser JE, Kerkhoff E, Mullins RD. Drosophila Spire is an actin nucleation factor. Nature. 2005 Jan 27;433(7024):382-8. PMID:15674283 doi:http://dx.doi.org/nature03241
↑ Ducka AM, Joel P, Popowicz GM, Trybus KM, Schleicher M, Noegel AA, Huber R, Holak TA, Sitar T. Structures of actin-bound Wiskott-Aldrich syndrome protein homology 2 (WH2) domains of Spire and the implication for filament nucleation. Proc Natl Acad Sci U S A. 2010 Jun 29;107(26):11757-62. Epub 2010 Jun 10. PMID:20538977 doi:10.1073/pnas.1005347107
↑ Vizcarra CL, Kreutz B, Rodal AA, Toms AV, Lu J, Zheng W, Quinlan ME, Eck MJ. Structure and function of the interacting domains of Spire and Fmn-family formins. Proc Natl Acad Sci U S A. 2011 Jul 19;108(29):11884-9. Epub 2011 Jul 5. PMID:21730168 doi:http://dx.doi.org/10.1073/pnas.1105703108
↑ Chen CK, Sawaya MR, Phillips ML, Reisler E, Quinlan ME. Multiple forms of Spire-actin complexes and their functional consequences. J Biol Chem. 2012 Feb 8. PMID:22334675 doi:10.1074/jbc.M111.317792

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/4efh"

@@ Line 1: / Line 1: @@
 ==Acanthamoeba Actin complex with Spir domain D==
 <StructureSection load='4efh' size='340' side='right' caption='[[4efh]], [[Resolution|resolution]] 2.48&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[4efh]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Acanthamoeba_castellanii Acanthamoeba castellanii] and [http://en.wikipedia.org/wiki/Drosophila_melanogaster Drosophila melanogaster]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4EFH OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4EFH FirstGlance]. <br>
+<table><tr><td colspan='2'>[[4efh]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Acanthamoeba_castellanii Acanthamoeba castellanii] and [http://en.wikipedia.org/wiki/Drome Drome]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4EFH OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4EFH FirstGlance]. <br>
 </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</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">[[3ue5|3ue5]]</td></tr>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">spir, p150-Spir, CG10076 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=7227 Drosophila melanogaster])</td></tr>
+<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">spir, p150-Spir, CG10076 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=7227 DROME])</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=4efh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4efh OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4efh RCSB], [http://www.ebi.ac.uk/pdbsum/4efh 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=4efh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4efh OCA], [http://pdbe.org/4efh PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4efh RCSB], [http://www.ebi.ac.uk/pdbsum/4efh PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4efh ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/SPIR_DROME SPIR_DROME]] Acts as an actin nucleation factor, remains associated with the slow-growing pointed end of the new filament. Promotes dissociation of capu from the barbed end of actin filaments. Involved in intracellular vesicle transport along actin fibers, providing a novel link between actin cytoskeleton dynamics and intracellular transport. Required for localization of determinants within the developing oocyte to the posterior pole and to the dorsal anterior corner. Links Rho family signaling and Jnk function to the actin cytoskeleton.<ref>PMID:10556052</ref> <ref>PMID:10744979</ref> <ref>PMID:15674283</ref> <ref>PMID:20538977</ref> <ref>PMID:21730168</ref>
+[[http://www.uniprot.org/uniprot/ACT1_ACACA ACT1_ACACA]] Actins are highly conserved proteins that are involved in various types of cell motility and are ubiquitously expressed in all eukaryotic cells. [[http://www.uniprot.org/uniprot/SPIR_DROME SPIR_DROME]] Acts as an actin nucleation factor, remains associated with the slow-growing pointed end of the new filament. Promotes dissociation of capu from the barbed end of actin filaments. Involved in intracellular vesicle transport along actin fibers, providing a novel link between actin cytoskeleton dynamics and intracellular transport. Required for localization of determinants within the developing oocyte to the posterior pole and to the dorsal anterior corner. Links Rho family signaling and Jnk function to the actin cytoskeleton.<ref>PMID:10556052</ref> <ref>PMID:10744979</ref> <ref>PMID:15674283</ref> <ref>PMID:20538977</ref> <ref>PMID:21730168</ref>
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
@@ Line 18: / Line 19: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 4efh" style="background-color:#fffaf0;"></div>
 ==See Also==
@@ Line 26: / Line 28: @@
 </StructureSection>
 [[Category: Acanthamoeba castellanii]]
-[[Category: Drosophila melanogaster]]
+[[Category: Drome]]
 [[Category: Chen, C]]
 [[Category: Phillips, M]]

4efh

From Proteopedia

Revision as of 20:39, 5 August 2016

Acanthamoeba Actin complex with Spir domain D

Structural highlights

Function

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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