4ai6: Difference between revisions

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-[[Image:4ai6.png|left|200px]]
-<!--
+==Dynein Motor Domain - ADP complex==
-The line below this paragraph, containing "STRUCTURE_4ai6", creates the "Structure Box" on the page.
+<StructureSection load='4ai6' size='340' side='right'caption='[[4ai6]], [[Resolution|resolution]] 3.40&Aring;' scene=''>
-You may change the PDB parameter (which sets the PDB file loaded into the applet)
+== Structural highlights ==
-or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
+<table><tr><td colspan='2'>[[4ai6]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae] and [https://en.wikipedia.org/wiki/Schistosoma_japonicum Schistosoma japonicum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4AI6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4AI6 FirstGlance]. <br>
-or leave the SCENE parameter empty for the default display.
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.4&#8491;</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=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
-{{STRUCTURE_4ai6|  PDB=4ai6  |  SCENE=  }}
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4ai6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ai6 OCA], [https://pdbe.org/4ai6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4ai6 RCSB], [https://www.ebi.ac.uk/pdbsum/4ai6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4ai6 ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/DYHC_YEAST DYHC_YEAST] Cytoplasmic dynein acts as a motor for the intracellular retrograde motility of vesicles and organelles along microtubules. Dynein has ATPase activity; the force-producing power stroke is thought to occur on release of ADP. Required to maintain uniform nuclear distribution in hyphae. May play an important role in the proper orientation of the mitotic spindle into the budding daughter cell yeast. Probably required for normal progression of the cell cycle.<ref>PMID:15642746</ref> [https://www.uniprot.org/uniprot/GST26_SCHJA GST26_SCHJA] Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles.  GST isoenzymes appear to play a central role in the parasite detoxification system. Other functions are also suspected including a role in increasing the solubility of haematin in the parasite gut.
+<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).
-===Dynein Motor Domain - ADP complex===
+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>
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
+<div class="pdbe-citations 4ai6" style="background-color:#fffaf0;"></div>
-<!--
+==See Also==
-The line below this paragraph, {{ABSTRACT_PUBMED_22426545}}, adds the Publication Abstract to the page
+*[[Dynein 3D structures|Dynein 3D structures]]
-(as it appears on PubMed at http://www.pubmed.gov), where 22426545 is the PubMed ID number.
+*[[Glutathione S-transferase 3D structures|Glutathione S-transferase 3D structures]]
--->
+== References ==
-{{ABSTRACT_PUBMED_22426545}}
+<references/>
+__TOC__
-==About this Structure==
+</StructureSection>
-[[4ai6]] 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=4AI6 OCA].
+[[Category: Large Structures]]
+[[Category: Saccharomyces cerevisiae]]
-==Reference==
+[[Category: Schistosoma japonicum]]
-<ref group="xtra">PMID:022426545</ref><references group="xtra"/>
+[[Category: Carter AP]]
-[[Category: Glutathione transferase]]
+[[Category: Gleave ES]]
-[[Category: Schistosoma japonicum, saccharomyces cerevisiae]]
+[[Category: Schmidt H]]
-[[Category: Carter, A P.]]
-[[Category: Gleave, E S.]]
-[[Category: Schmidt, H.]]
-[[Category: Aaa+ protein]]
-[[Category: Asce protein]]
-[[Category: Atpase]]
-[[Category: Cytoskeletal motor]]
-[[Category: Motor protein]]
-[[Category: P-loop ntpase]]