1y64

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[[Image:1y64.png|left|200px]]
 
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==Bni1p Formin Homology 2 Domain complexed with ATP-actin==
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The line below this paragraph, containing "STRUCTURE_1y64", creates the "Structure Box" on the page.
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<StructureSection load='1y64' size='340' side='right'caption='[[1y64]], [[Resolution|resolution]] 3.05&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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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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</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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<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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{{STRUCTURE_1y64| PDB=1y64 | SCENE= }}
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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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(as it appears on PubMed at http://www.pubmed.gov), where 15635372 is the PubMed ID number.
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{{ABSTRACT_PUBMED_15635372}}
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==About this Structure==
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[[1y64]] is a 2 chain structure of [[Actin]] with sequence 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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==See Also==
==See Also==
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*[[Actin]]
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*[[Actin 3D structures|Actin 3D structures]]
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== References ==
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==Reference==
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<references/>
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<ref group="xtra">PMID:15635372</ref><references group="xtra"/>
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__TOC__
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</StructureSection>
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[[Category: Large Structures]]
[[Category: Oryctolagus cuniculus]]
[[Category: Oryctolagus cuniculus]]
[[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: 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: Structural protein]]
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[[Category: Tetramethylrhodamine-5-maleimide]]
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Current revision

Bni1p Formin Homology 2 Domain complexed with ATP-actin

PDB ID 1y64

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