4eah: Difference between revisions

From Proteopedia
Jump to navigation Jump to search
← Older editNewer edit →
No edit summary
No edit summary
Line 1: Line 1:


==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==
<StructureSection load='4eah' size='340' side='right' caption='[[4eah]], [[Resolution|resolution]] 3.40&Aring;' scene=''>
<StructureSection load='4eah' size='340' side='right'caption='[[4eah]], [[Resolution|resolution]] 3.40&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<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>
<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>
</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>
</td></tr><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>
<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>
<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>
<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>
</table>
</table>
== Function ==
== Function ==
[[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).  
[[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.
<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
Line 19: Line 18:
</div>
</div>
<div class="pdbe-citations 4eah" style="background-color:#fffaf0;"></div>
<div class="pdbe-citations 4eah" style="background-color:#fffaf0;"></div>
==See Also==
*[[Actin 3D structures|Actin 3D structures]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Lk3 transgenic mice]]
[[Category: Large Structures]]
[[Category: Mus musculus]]
[[Category: Oryctolagus cuniculus]]
[[Category: Oryctolagus cuniculus]]
[[Category: Gauvin, T J]]
[[Category: Gauvin TJ]]
[[Category: Heimsath, E G]]
[[Category: Heimsath EG]]
[[Category: Higgs, H N]]
[[Category: Higgs HN]]
[[Category: Kull, F J]]
[[Category: Kull FJ]]
[[Category: Thompson, M E]]
[[Category: Thompson ME]]
[[Category: Actin]]
[[Category: Atp binding]]
[[Category: Cytoskeleton]]
[[Category: Fmnl3]]
[[Category: Formin]]
[[Category: Protein binding]]

Revision as of 10:00, 28 September 2022

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

Structural highlights

4eah is a 8 chain structure with sequence from Mus musculus and Oryctolagus cuniculus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:,
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.

Publication Abstract from PubMed

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.

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[1]

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

See Also

References

  1. ↑ Thompson ME, Heimsath EG, Gauvin TJ, Higgs HN, Kull FJ. FMNL3 FH2-actin structure gives insight into formin-mediated actin nucleation and elongation. Nat Struct Mol Biol. 2012 Dec 9. doi: 10.1038/nsmb.2462. PMID:23222643 doi:http://dx.doi.org/10.1038/nsmb.2462

4eah, resolution 3.40Å

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA
Retrieved from "https://proteopedia.openfox.io/wiki/index.php?title=4eah&oldid=3639086"