1jx2: Difference between revisions

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-[[Image:1jx2.png|left|200px]]
-<!--
+==CRYSTAL STRUCTURE OF THE NUCLEOTIDE-FREE DYNAMIN A GTPASE DOMAIN, DETERMINED AS MYOSIN FUSION==
-The line below this paragraph, containing "STRUCTURE_1jx2", creates the "Structure Box" on the page.
+<StructureSection load='1jx2' size='340' side='right'caption='[[1jx2]], [[Resolution|resolution]] 2.30&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'>[[1jx2]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Dictyostelium_discoideum Dictyostelium discoideum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JX2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1JX2 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]] 2.3&#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=BGC:BETA-D-GLUCOSE'>BGC</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
-{{STRUCTURE_1jx2|  PDB=1jx2  |  SCENE=  }}
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1jx2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1jx2 OCA], [https://pdbe.org/1jx2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1jx2 RCSB], [https://www.ebi.ac.uk/pdbsum/1jx2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1jx2 ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/DYNA_DICDI DYNA_DICDI] Function in membrane trafficking processes along the endo-lysosomal pathway.[https://www.uniprot.org/uniprot/MYS2_DICDI MYS2_DICDI] Myosin is a protein that binds to actin and has ATPase activity that is activated by actin.
+== Evolutionary Conservation ==
+[[Image:Consurf_key_small.gif|200px|right]]
+Check<jmol>
+  <jmolCheckbox>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/jx/1jx2_consurf.spt"</scriptWhenChecked>
+    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
+    <text>to colour the structure by Evolutionary Conservation</text>
+  </jmolCheckbox>
+</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1jx2 ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+Dynamins form a family of multidomain GTPases involved in endocytosis, vesicle trafficking and maintenance of mitochondrial morphology. In contrast to the classical switch GTPases, a force-generating function has been suggested for dynamins. Here we report the 2.3 A crystal structure of the nucleotide-free and GDP-bound GTPase domain of Dictyostelium discoideum dynamin A. The GTPase domain is the most highly conserved region among dynamins. The globular structure contains the G-protein core fold, which is extended from a six-stranded beta-sheet to an eight-stranded one by a 55 amino acid insertion. This topologically unique insertion distinguishes dynamins from other subfamilies of GTP-binding proteins. An additional N-terminal helix interacts with the C-terminal helix of the GTPase domain, forming a hydrophobic groove, which could be occupied by C-terminal parts of dynamin not present in our construct. The lack of major conformational changes between the nucleotide-free and the GDP-bound state suggests that mechanochemical rearrangements in dynamin occur during GTP binding, GTP hydrolysis or phosphate release and are not linked to loss of GDP.
-===CRYSTAL STRUCTURE OF THE NUCLEOTIDE-FREE DYNAMIN A GTPASE DOMAIN, DETERMINED AS MYOSIN FUSION===
+Crystal structure of a dynamin GTPase domain in both nucleotide-free and GDP-bound forms.,Niemann HH, Knetsch ML, Scherer A, Manstein DJ, Kull FJ EMBO J. 2001 Nov 1;20(21):5813-21. PMID:11689422<ref>PMID:11689422</ref>
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-<!--
+</div>
-The line below this paragraph, {{ABSTRACT_PUBMED_11689422}}, adds the Publication Abstract to the page
+<div class="pdbe-citations 1jx2" style="background-color:#fffaf0;"></div>
-(as it appears on PubMed at http://www.pubmed.gov), where 11689422 is the PubMed ID number.
--->
-{{ABSTRACT_PUBMED_11689422}}
-==About this Structure==
-[[1jx2]] is a 3 chain structure of [[Myosin]] with sequence from [http://en.wikipedia.org/wiki/Dictyostelium_discoideum Dictyostelium discoideum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JX2 OCA].
 ==See Also==
-*[[Myosin]]
+*[[Myosin 3D Structures|Myosin 3D Structures]]
+== References ==
-==Reference==
+<references/>
-<ref group="xtra">PMID:11689422</ref><references group="xtra"/>
+__TOC__
+</StructureSection>
 [[Category: Dictyostelium discoideum]]
-[[Category: Knetsch, M L.W.]]
+[[Category: Large Structures]]
-[[Category: Kull, F J.]]
+[[Category: Knetsch MLW]]
-[[Category: Manstein, D J.]]
+[[Category: Kull FJ]]
-[[Category: Niemann, H H.]]
+[[Category: Manstein DJ]]
-[[Category: Scherer, A.]]
+[[Category: Niemann HH]]
-[[Category: Dictyostelium]]
+[[Category: Scherer A]]
-[[Category: Dynamin]]
-[[Category: Fusion-protein]]
-[[Category: Gtpase]]
-[[Category: Hydrolase]]
-[[Category: Myosin]]