1y64

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[[Image:1y64.gif|left|200px]]
 
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{{Structure
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==Bni1p Formin Homology 2 Domain complexed with ATP-actin==
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|PDB= 1y64 |SIZE=350|CAPTION= <scene name='initialview01'>1y64</scene>, resolution 3.05&Aring;
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<StructureSection load='1y64' size='340' side='right'caption='[[1y64]], [[Resolution|resolution]] 3.05&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene> and <scene name='pdbligand=ATP:ADENOSINE-5'-TRIPHOSPHATE'>ATP</scene>
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<table><tr><td colspan='2'>[[1y64]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Oryctolagus_cuniculus Oryctolagus cuniculus] and [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Y64 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1Y64 FirstGlance]. <br>
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|ACTIVITY=
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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]] 3.05&#8491;</td></tr>
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|GENE= BNI1, PPF3, SHE5 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 Saccharomyces cerevisiae])
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=HIC:4-METHYL-HISTIDINE'>HIC</scene></td></tr>
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}}
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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=1y64 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1y64 OCA], [https://pdbe.org/1y64 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1y64 RCSB], [https://www.ebi.ac.uk/pdbsum/1y64 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1y64 ProSAT]</span></td></tr>
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</table>
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== Function ==
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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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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/y6/1y64_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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=1y64 ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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The conserved formin homology 2 (FH2) domain nucleates actin filaments and remains bound to the barbed end of the growing filament. Here we report the crystal structure of the yeast Bni1p FH2 domain in complex with tetramethylrhodamine-actin. Each of the two structural units in the FH2 dimer binds two actins in an orientation similar to that in an actin filament, suggesting that this structure could function as a filament nucleus. Biochemical properties of heterodimeric FH2 mutants suggest that the wild-type protein equilibrates between two bound states at the barbed end: one permitting monomer binding and the other permitting monomer dissociation. Interconversion between these states allows processive barbed-end polymerization and depolymerization in the presence of bound FH2 domain. Kinetic and/or thermodynamic differences in the conformational and binding equilibria can explain the variable activity of different FH2 domains as well as the effects of the actin-binding protein profilin on FH2 function.
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'''Bni1p Formin Homology 2 Domain complexed with ATP-actin'''
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Structural basis of actin filament nucleation and processive capping by a formin homology 2 domain.,Otomo T, Tomchick DR, Otomo C, Panchal SC, Machius M, Rosen MK Nature. 2005 Feb 3;433(7025):488-94. Epub 2005 Jan 5. PMID:15635372<ref>PMID:15635372</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 1y64" style="background-color:#fffaf0;"></div>
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==Overview==
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==See Also==
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The conserved formin homology 2 (FH2) domain nucleates actin filaments and remains bound to the barbed end of the growing filament. Here we report the crystal structure of the yeast Bni1p FH2 domain in complex with tetramethylrhodamine-actin. Each of the two structural units in the FH2 dimer binds two actins in an orientation similar to that in an actin filament, suggesting that this structure could function as a filament nucleus. Biochemical properties of heterodimeric FH2 mutants suggest that the wild-type protein equilibrates between two bound states at the barbed end: one permitting monomer binding and the other permitting monomer dissociation. Interconversion between these states allows processive barbed-end polymerization and depolymerization in the presence of bound FH2 domain. Kinetic and/or thermodynamic differences in the conformational and binding equilibria can explain the variable activity of different FH2 domains as well as the effects of the actin-binding protein profilin on FH2 function.
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*[[Actin 3D structures|Actin 3D structures]]
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== References ==
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==About this Structure==
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<references/>
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1Y64 is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Oryctolagus_cuniculus Oryctolagus cuniculus] and [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Y64 OCA].
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__TOC__
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</StructureSection>
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==Reference==
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[[Category: Large Structures]]
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Structural basis of actin filament nucleation and processive capping by a formin homology 2 domain., Otomo T, Tomchick DR, Otomo C, Panchal SC, Machius M, Rosen MK, Nature. 2005 Feb 3;433(7025):488-94. Epub 2005 Jan 5. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15635372 15635372]
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[[Category: Oryctolagus cuniculus]]
[[Category: Oryctolagus cuniculus]]
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[[Category: Protein complex]]
 
[[Category: Saccharomyces cerevisiae]]
[[Category: Saccharomyces cerevisiae]]
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[[Category: Machius, M.]]
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[[Category: Machius M]]
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[[Category: Otomo, C.]]
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[[Category: Otomo C]]
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[[Category: Otomo, T.]]
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[[Category: Otomo T]]
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[[Category: Panchal, S C.]]
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[[Category: Panchal SC]]
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[[Category: Rosen, M K.]]
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[[Category: Rosen MK]]
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[[Category: Tomchick, D R.]]
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[[Category: Tomchick DR]]
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[[Category: ATP]]
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[[Category: CA]]
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[[Category: actin]]
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[[Category: atp-state]]
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[[Category: coiled coil]]
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[[Category: fh2 actin cytoskeleton]]
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[[Category: tetramethylrhodamine-5-maleimide]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 15:18:51 2008''
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Current revision

Bni1p Formin Homology 2 Domain complexed with ATP-actin

PDB ID 1y64

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