1j6z
From Proteopedia
(Difference between revisions)
m (Protected "1j6z" [edit=sysop:move=sysop]) |
|||
| (9 intermediate revisions not shown.) | |||
| Line 1: | Line 1: | ||
| - | [[Image:1j6z.png|left|200px]] | ||
| - | + | ==UNCOMPLEXED ACTIN== | |
| + | <StructureSection load='1j6z' size='340' side='right'caption='[[1j6z]], [[Resolution|resolution]] 1.54Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[1j6z]] 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=1J6Z OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1J6Z FirstGlance]. <br> | ||
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.54Å</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=HIC:4-METHYL-HISTIDINE'>HIC</scene>, <scene name='pdbligand=RHO:TETRAMETHYLRHODAMINE-5-MALEIMIDE'>RHO</scene></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=1j6z FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1j6z OCA], [https://pdbe.org/1j6z PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1j6z RCSB], [https://www.ebi.ac.uk/pdbsum/1j6z PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1j6z ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == 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 == | ||
| + | The dynamics and polarity of actin filaments are controlled by a conformational change coupled to the hydrolysis of adenosine 5'-triphosphate (ATP) by a mechanism that remains to be elucidated. Actin modified to block polymerization was crystallized in the adenosine 5'-diphosphate (ADP) state, and the structure was solved to 1.54 angstrom resolution. Compared with previous ATP-actin structures from complexes with deoxyribonuclease I, profilin, and gelsolin, monomeric ADP-actin is characterized by a marked conformational change in subdomain 2. The successful crystallization of monomeric actin opens the way to future structure determinations of actin complexes with actin-binding proteins such as myosin. | ||
| - | + | The crystal structure of uncomplexed actin in the ADP state.,Otterbein LR, Graceffa P, Dominguez R Science. 2001 Jul 27;293(5530):708-11. PMID:11474115<ref>PMID:11474115</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | <div class="pdbe-citations 1j6z" style="background-color:#fffaf0;"></div> | |
| - | + | ||
==See Also== | ==See Also== | ||
| - | *[[Actin|Actin]] | + | *[[Actin 3D structures|Actin 3D structures]] |
| - | + | == References == | |
| - | + | <references/> | |
| - | == | + | __TOC__ |
| - | < | + | </StructureSection> |
| + | [[Category: Large Structures]] | ||
[[Category: Oryctolagus cuniculus]] | [[Category: Oryctolagus cuniculus]] | ||
| - | [[Category: Dominguez | + | [[Category: Dominguez R]] |
| - | [[Category: Graceffa | + | [[Category: Graceffa P]] |
| - | [[Category: Otterbein | + | [[Category: Otterbein LR]] |
| - | + | ||
| - | + | ||
| - | + | ||
| - | + | ||
Current revision
UNCOMPLEXED ACTIN
| |||||||||||
