1lcu: Difference between revisions

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-[[Image:1lcu.jpg|left|200px]]
- {{Structure
+==Polylysine Induces an Antiparallel Actin Dimer that Nucleates Filament Assembly: Crystal Structure at 3.5 A Resolution==
-|PDB= 1lcu |SIZE=350|CAPTION= <scene name='initialview01'>1lcu</scene>, resolution 3.5&Aring;
+<StructureSection load='1lcu' size='340' side='right'caption='[[1lcu]], [[Resolution|resolution]] 3.50&Aring;' scene=''>
-|SITE=
+== Structural highlights ==
-|LIGAND= <scene name='pdbligand=ATP:ADENOSINE-5&#39;-TRIPHOSPHATE'>ATP</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=LAR:LATRUNCULIN+A'>LAR</scene>
+<table><tr><td colspan='2'>[[1lcu]] is a 2 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=1LCU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1LCU FirstGlance]. <br>
-|ACTIVITY=
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.5&#8491;</td></tr>
-|GENE=
+<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=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=LAR:LATRUNCULIN+A'>LAR</scene></td></tr>
-|DOMAIN=
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1lcu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1lcu OCA], [https://pdbe.org/1lcu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1lcu RCSB], [https://www.ebi.ac.uk/pdbsum/1lcu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1lcu ProSAT]</span></td></tr>
-|RELATEDENTRY=
+</table>
-|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1lcu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1lcu OCA], [http://www.ebi.ac.uk/pdbsum/1lcu PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1lcu RCSB]</span>
+== Function ==
-}}
+[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;">
+== Publication Abstract from PubMed ==
+An antiparallel actin dimer has been proposed to be an intermediate species during actin filament nucleation. We now show that latrunculin A, a marine natural product that inhibits actin polymerization, arrests polylysine-induced nucleation at the level of an antiparallel dimer, resulting in its accumulation. These dimers, when composed of pyrene-labeled actin subunits, give rise to a fluorescent excimer, permitting detection during polymerization in vitro. We report the crystallographic structure of the polylysine-actin-latrunculin A complex at 3.5-A resolution. The non-crystallographic contact is consistent with a dimeric structure and confirms the antiparallel orientation of its subunits. The crystallographic contacts reveal that the mobile DNase I binding loop of one subunit of a symmetry-related antiparallel actin dimer is partially stabilized in the interface between the two subunits of a second antiparallel dimer. These results provide a potential explanation for the paradoxical nucleation of actin filaments that have exclusively parallel subunits by a dimer containing antiparallel subunits.
-'''Polylysine Induces an Antiparallel Actin Dimer that Nucleates Filament Assembly: Crystal Structure at 3.5 A Resolution'''
+Polylysine induces an antiparallel actin dimer that nucleates filament assembly: crystal structure at 3.5-A resolution.,Bubb MR, Govindasamy L, Yarmola EG, Vorobiev SM, Almo SC, Somasundaram T, Chapman MS, Agbandje-McKenna M, McKenna R J Biol Chem. 2002 Jun 7;277(23):20999-1006. Epub 2002 Apr 3. PMID:11932258<ref>PMID:11932258</ref>
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
+<div class="pdbe-citations 1lcu" style="background-color:#fffaf0;"></div>
-==Overview==
+==See Also==
-An antiparallel actin dimer has been proposed to be an intermediate species during actin filament nucleation. We now show that latrunculin A, a marine natural product that inhibits actin polymerization, arrests polylysine-induced nucleation at the level of an antiparallel dimer, resulting in its accumulation. These dimers, when composed of pyrene-labeled actin subunits, give rise to a fluorescent excimer, permitting detection during polymerization in vitro. We report the crystallographic structure of the polylysine-actin-latrunculin A complex at 3.5-A resolution. The non-crystallographic contact is consistent with a dimeric structure and confirms the antiparallel orientation of its subunits. The crystallographic contacts reveal that the mobile DNase I binding loop of one subunit of a symmetry-related antiparallel actin dimer is partially stabilized in the interface between the two subunits of a second antiparallel dimer. These results provide a potential explanation for the paradoxical nucleation of actin filaments that have exclusively parallel subunits by a dimer containing antiparallel subunits.
+*[[Actin 3D structures|Actin 3D structures]]
+== References ==
-==About this Structure==
+<references/>
-LCU 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=1LCU OCA].
+__TOC__
+</StructureSection>
-==Reference==
+[[Category: Large Structures]]
-Polylysine induces an antiparallel actin dimer that nucleates filament assembly: crystal structure at 3.5-A resolution., Bubb MR, Govindasamy L, Yarmola EG, Vorobiev SM, Almo SC, Somasundaram T, Chapman MS, Agbandje-McKenna M, McKenna R, J Biol Chem. 2002 Jun 7;277(23):20999-1006. Epub 2002 Apr 3. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11932258 11932258]
 [[Category: Oryctolagus cuniculus]]
-[[Category: Single protein]]
+[[Category: Agbandje-Mckenna M]]
-[[Category: Agbandje-Mckenna, M.]]
+[[Category: Almo SC]]
-[[Category: Almo, S C.]]
+[[Category: Bubb MR]]
-[[Category: Bubb, M R.]]
+[[Category: Chapman MS]]
-[[Category: Chapman, M S.]]
+[[Category: Govindasamy L]]
-[[Category: Govindasamy, L.]]
+[[Category: Mckenna R]]
-[[Category: Mckenna, R.]]
+[[Category: Somasundaram T]]
-[[Category: Somasundaram, T.]]
+[[Category: Vorobiev SM]]
-[[Category: Vorobiev, S M.]]
+[[Category: Yarmola EG]]
-[[Category: Yarmola, E G.]]
-[[Category: muscle protein]]
-[[Category: structural protein]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:01:11 2008''