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3mn5

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Revision as of 21:00, 5 August 2016

Structures of actin-bound WH2 domains of Spire and the implication for filament nucleation

Structural highlights

3mn5 is a 2 chain structure with sequence from Drome and Oryctolagus cuniculus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	, ,
Related:	1ijj, 3mmv, 3mn6, 3mn7, 3mn9
Gene:	spir, p150-Spir, CG10076 (DROME)
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[ACTS_RABIT] 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]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

Three classes of proteins are known to nucleate new filaments: the Arp2/3 complex, formins, and the third group of proteins that contain ca. 25 amino acid long actin-binding Wiskott-Aldrich syndrome protein homology 2 domains, called the WH2 repeats. Crystal structures of the complexes between the actin-binding WH2 repeats of the Spire protein and actin were determined for the Spire single WH2 domain D, the double (SpirCD), triple (SpirBCD), quadruple (SpirABCD) domains, and an artificial Spire WH2 construct comprising three identical D repeats (SpirDDD). SpirCD represents the minimal functional core of Spire that can nucleate actin filaments. Packing in the crystals of the actin complexes with SpirCD, SpirBCD, SpirABCD, and SpirDDD shows the presence of two types of assemblies, "side-to-side" and "straight-longitudinal," which can serve as actin filament nuclei. The principal feature of these structures is their loose, open conformations, in which the sides of actins that normally constitute the inner interface core of a filament are flipped inside out. These Spire structures are distant from those seen in the filamentous nuclei of Arp2/3, formins, and in the F-actin filament.

Structures of actin-bound Wiskott-Aldrich syndrome protein homology 2 (WH2) domains of Spire and the implication for filament nucleation.,Ducka AM, Joel P, Popowicz GM, Trybus KM, Schleicher M, Noegel AA, Huber R, Holak TA, Sitar T Proc Natl Acad Sci U S A. 2010 Jun 29;107(26):11757-62. Epub 2010 Jun 10. PMID:20538977^[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
↑ 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

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/3mn5"

@@ Line 1: / Line 1: @@
 ==Structures of actin-bound WH2 domains of Spire and the implication for filament nucleation==
 <StructureSection load='3mn5' size='340' side='right' caption='[[3mn5]], [[Resolution|resolution]] 1.50&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[3mn5]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Drosophila_melanogaster Drosophila melanogaster] and [http://en.wikipedia.org/wiki/Oryctolagus_cuniculus Oryctolagus cuniculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3MN5 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3MN5 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[3mn5]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Drome Drome] and [http://en.wikipedia.org/wiki/Oryctolagus_cuniculus Oryctolagus cuniculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3MN5 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3MN5 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>, <scene name='pdbligand=LAB:LATRUNCULIN+B'>LAB</scene></td></tr>
 <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1ijj|1ijj]], [[3mmv|3mmv]], [[3mn6|3mn6]], [[3mn7|3mn7]], [[3mn9|3mn9]]</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=3mn5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3mn5 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3mn5 RCSB], [http://www.ebi.ac.uk/pdbsum/3mn5 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=3mn5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3mn5 OCA], [http://pdbe.org/3mn5 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3mn5 RCSB], [http://www.ebi.ac.uk/pdbsum/3mn5 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3mn5 ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 18: / Line 19: @@
     <text>to colour the structure by Evolutionary Conservation</text>
   </jmolCheckbox>
-</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/chain_selection.php?pdb_ID=2ata ConSurf].
+</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=3mn5 ConSurf].
 <div style="clear:both"></div>
 <div style="background-color:#fffaf0;">
@@ Line 28: / Line 29: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 3mn5" style="background-color:#fffaf0;"></div>
 ==See Also==
@@ Line 35: / Line 37: @@
 __TOC__
 </StructureSection>
-[[Category: Drosophila melanogaster]]
+[[Category: Drome]]
 [[Category: Oryctolagus cuniculus]]
 [[Category: Ducka, A M]]

3mn5

From Proteopedia

Revision as of 21:00, 5 August 2016

Structures of actin-bound WH2 domains of Spire and the implication for filament nucleation

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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