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2fxu

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[[Image:2fxu.gif|left|200px]]
 
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{{Structure
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==X-ray Structure of Bistramide A- Actin Complex at 1.35 A resolution.==
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|PDB= 2fxu |SIZE=350|CAPTION= <scene name='initialview01'>2fxu</scene>, resolution 1.35&Aring;
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<StructureSection load='2fxu' size='340' side='right'caption='[[2fxu]], [[Resolution|resolution]] 1.35&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND= <scene name='pdbligand=ATP:ADENOSINE-5&#39;-TRIPHOSPHATE'>ATP</scene>, <scene name='pdbligand=BID:BISTRAMIDE+A'>BID</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=HIC:4-METHYL-HISTIDINE'>HIC</scene>
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<table><tr><td colspan='2'>[[2fxu]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Oryctolagus_cuniculus Oryctolagus cuniculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2FXU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2FXU 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]] 1.35&#8491;</td></tr>
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|GENE=
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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=BID:BISTRAMIDE+A'>BID</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=HIC:4-METHYL-HISTIDINE'>HIC</scene></td></tr>
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|DOMAIN=
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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=2fxu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2fxu OCA], [https://pdbe.org/2fxu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2fxu RCSB], [https://www.ebi.ac.uk/pdbsum/2fxu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2fxu ProSAT]</span></td></tr>
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|RELATEDENTRY=
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</table>
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2fxu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2fxu OCA], [http://www.ebi.ac.uk/pdbsum/2fxu PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2fxu RCSB]</span>
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== Function ==
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}}
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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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Bistramide A is a highly potent antiproliferative marine natural product from Lissoclinum bistratum. We have previously established actin as the primary cellular receptor of bistramide A. We report herein the X-ray structure of bistramide A bound to monomeric actin at a resolution of 1.35 A. The most notable aspect of the bistramide A-actin structure is an extensive hydrogen-bonding network established upon a deep penetration of the central segment of bistramide A into the actin-binding cleft between subdomains 1 and 3. The structure presents the first insight into the observed ability of bistramide A to modulate G-actin polymerization. The structural information combined with our ability to chemically modify the bistramide framework provides the basis for rational development of a series of new synthetic analogues as useful probes for studying actin cytoskeleton and as potential therapeutic leads.
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'''X-ray Structure of Bistramide A- Actin Complex at 1.35 A resolution.'''
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Structure of bistramide A-actin complex at a 1.35 angstroms resolution.,Rizvi SA, Tereshko V, Kossiakoff AA, Kozmin SA J Am Chem Soc. 2006 Mar 29;128(12):3882-3. PMID:16551075<ref>PMID:16551075</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 2fxu" style="background-color:#fffaf0;"></div>
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==Overview==
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==See Also==
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Bistramide A is a highly potent antiproliferative marine natural product from Lissoclinum bistratum. We have previously established actin as the primary cellular receptor of bistramide A. We report herein the X-ray structure of bistramide A bound to monomeric actin at a resolution of 1.35 A. The most notable aspect of the bistramide A-actin structure is an extensive hydrogen-bonding network established upon a deep penetration of the central segment of bistramide A into the actin-binding cleft between subdomains 1 and 3. The structure presents the first insight into the observed ability of bistramide A to modulate G-actin polymerization. The structural information combined with our ability to chemically modify the bistramide framework provides the basis for rational development of a series of new synthetic analogues as useful probes for studying actin cytoskeleton and as potential therapeutic leads.
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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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2FXU is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Oryctolagus_cuniculus Oryctolagus cuniculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2FXU 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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Structure of bistramide A-actin complex at a 1.35 angstroms resolution., Rizvi SA, Tereshko V, Kossiakoff AA, Kozmin SA, J Am Chem Soc. 2006 Mar 29;128(12):3882-3. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16551075 16551075]
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[[Category: Oryctolagus cuniculus]]
[[Category: Oryctolagus cuniculus]]
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[[Category: Single protein]]
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[[Category: Kossiakoff AA]]
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[[Category: Kossiakoff, A A.]]
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[[Category: Kozmin SA]]
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[[Category: Kozmin, S A.]]
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[[Category: Rizvi SA]]
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[[Category: Rizvi, S A.]]
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[[Category: Tereshko V]]
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[[Category: Tereshko, V.]]
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[[Category: actin complexed to bistramide some]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 03:09:07 2008''
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Current revision

X-ray Structure of Bistramide A- Actin Complex at 1.35 A resolution.

PDB ID 2fxu

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