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4akh
From Proteopedia
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| - | [[ | + | ==Dynein Motor Domain - AMPPNP complex== |
| + | <StructureSection load='4akh' size='340' side='right' caption='[[4akh]], [[Resolution|resolution]] 3.60Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[4akh]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Schistosoma_japonicum,_saccharomyces_cerevisiae Schistosoma japonicum, saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4AKH OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4AKH FirstGlance]. <br> | ||
| + | </td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ANP:PHOSPHOAMINOPHOSPHONIC+ACID-ADENYLATE+ESTER'>ANP</scene>, <scene name='pdbligand=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene><br> | ||
| + | <tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1b8x|1b8x]], [[1dug|1dug]], [[1gne|1gne]], [[1gta|1gta]], [[1gtb|1gtb]], [[1m99|1m99]], [[1m9a|1m9a]], [[1m9b|1m9b]], [[1u87|1u87]], [[1u88|1u88]], [[1ua5|1ua5]], [[1y6e|1y6e]], [[4ai6|4ai6]], [[4akg|4akg]], [[4aki|4aki]]</td></tr> | ||
| + | <tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Glutathione_transferase Glutathione transferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.5.1.18 2.5.1.18] </span></td></tr> | ||
| + | <tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4akh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4akh OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4akh RCSB], [http://www.ebi.ac.uk/pdbsum/4akh PDBsum]</span></td></tr> | ||
| + | <table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Dyneins power the beating of cilia and flagella, transport various intracellular cargos and are necessary for mitosis. All dyneins have a approximately 300-kDa motor domain consisting of a ring of six AAA+ domains. ATP hydrolysis in the AAA+ ring drives the cyclic relocation of a motile element, the linker domain, to generate the force necessary for movement. How the linker interacts with the ring during the ATP hydrolysis cycle is not known. Here we present a 3.3-A crystal structure of the motor domain of Saccharomyces cerevisiae cytoplasmic dynein, crystallized in the absence of nucleotides. The linker is docked to a conserved site on AAA5, which is confirmed by mutagenesis as functionally necessary. Nucleotide soaking experiments show that the main ATP hydrolysis site in dynein (AAA1) is in a low-nucleotide affinity conformation and reveal the nucleotide interactions of the other three sites (AAA2, AAA3 and AAA4). | ||
| - | + | Insights into dynein motor domain function from a 3.3-A crystal structure.,Schmidt H, Gleave ES, Carter AP Nat Struct Mol Biol. 2012 Mar 14;19(5):492-7. doi: 10.1038/nsmb.2272. PMID:22426545<ref>PMID:22426545</ref> | |
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| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| + | </div> | ||
| - | + | ==See Also== | |
| - | + | *[[Dynein|Dynein]] | |
| - | + | *[[Glutathione S-transferase|Glutathione S-transferase]] | |
| - | + | == References == | |
| - | + | <references/> | |
| - | + | __TOC__ | |
| - | + | </StructureSection> | |
| - | == | + | |
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[[Category: Glutathione transferase]] | [[Category: Glutathione transferase]] | ||
[[Category: Schistosoma japonicum, saccharomyces cerevisiae]] | [[Category: Schistosoma japonicum, saccharomyces cerevisiae]] | ||
Revision as of 07:20, 5 June 2014
Dynein Motor Domain - AMPPNP complex
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