4eah

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==Crystal structure of the formin homology 2 domain of FMNL3 bound to actin==
==Crystal structure of the formin homology 2 domain of FMNL3 bound to actin==
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<StructureSection load='4eah' size='340' side='right' caption='[[4eah]], [[Resolution|resolution]] 3.40&Aring;' scene=''>
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<StructureSection load='4eah' size='340' side='right'caption='[[4eah]], [[Resolution|resolution]] 3.40&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[4eah]] is a 8 chain structure with sequence from [http://en.wikipedia.org/wiki/Lk3_transgenic_mice Lk3 transgenic mice] 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=4EAH OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4EAH FirstGlance]. <br>
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<table><tr><td colspan='2'>[[4eah]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus] and [https://en.wikipedia.org/wiki/Oryctolagus_cuniculus Oryctolagus cuniculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4EAH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4EAH FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.4&#8491;</td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Fmnl3, Kiaa2014 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 LK3 transgenic mice])</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</scene></td></tr>
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<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=4eah FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4eah OCA], [http://pdbe.org/4eah PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4eah RCSB], [http://www.ebi.ac.uk/pdbsum/4eah PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4eah ProSAT]</span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4eah FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4eah OCA], [https://pdbe.org/4eah PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4eah RCSB], [https://www.ebi.ac.uk/pdbsum/4eah PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4eah ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/ACTS_RABIT ACTS_RABIT]] 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/FMNL3_MOUSE FMNL3_MOUSE]] Plays a role in the regulation of cell morphology and cytoskeletal organization. Required in the control of cell shape and migration (By similarity).
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[https://www.uniprot.org/uniprot/ACTS_RABIT ACTS_RABIT] Actins are highly conserved proteins that are involved in various types of cell motility and are ubiquitously expressed in all eukaryotic cells.
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Formins are actin-assembly factors that act in a variety of actin-based processes. The conserved formin homology 2 (FH2) domain promotes filament nucleation and influences elongation through interaction with the barbed end. FMNL3 is a formin that induces assembly of filopodia but whose FH2 domain is a poor nucleator. The 3.4-A structure of a mouse FMNL3 FH2 dimer in complex with tetramethylrhodamine-actin uncovers details of formin-regulated actin elongation. We observe distinct FH2 actin-binding regions; interactions in the knob and coiled-coil subdomains are necessary for actin binding, whereas those in the lasso-post interface are important for the stepping mechanism. Biochemical and cellular experiments test the importance of individual residues for function. This structure provides details for FH2-mediated filament elongation by processive capping and supports a model in which C-terminal non-FH2 residues of FMNL3 are required to stabilize the filament nucleus.
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FMNL3 FH2-actin structure gives insight into formin-mediated actin nucleation and elongation.,Thompson ME, Heimsath EG, Gauvin TJ, Higgs HN, Kull FJ Nat Struct Mol Biol. 2012 Dec 9. doi: 10.1038/nsmb.2462. PMID:23222643<ref>PMID:23222643</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 4eah" style="background-color:#fffaf0;"></div>
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==See Also==
==See Also==
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*[[Actin|Actin]]
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*[[Actin 3D structures|Actin 3D structures]]
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Lk3 transgenic mice]]
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[[Category: Large Structures]]
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[[Category: Mus musculus]]
[[Category: Oryctolagus cuniculus]]
[[Category: Oryctolagus cuniculus]]
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[[Category: Gauvin, T J]]
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[[Category: Gauvin TJ]]
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[[Category: Heimsath, E G]]
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[[Category: Heimsath EG]]
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[[Category: Higgs, H N]]
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[[Category: Higgs HN]]
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[[Category: Kull, F J]]
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[[Category: Kull FJ]]
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[[Category: Thompson, M E]]
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[[Category: Thompson ME]]
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[[Category: Actin]]
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[[Category: Atp binding]]
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[[Category: Cytoskeleton]]
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[[Category: Fmnl3]]
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[[Category: Formin]]
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[[Category: Protein binding]]
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Current revision

Crystal structure of the formin homology 2 domain of FMNL3 bound to actin

PDB ID 4eah

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