1ia0: Difference between revisions

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-[[Image:1ia0.gif|left|200px]]
-<!--
-The line below this paragraph, containing "STRUCTURE_1ia0", creates the "Structure Box" on the page.
-You may change the PDB parameter (which sets the PDB file loaded into the applet)
-or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
-or leave the SCENE parameter empty for the default display.
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-{{STRUCTURE_1ia0|  PDB=1ia0  |  SCENE=  }}
-'''KIF1A HEAD-MICROTUBULE COMPLEX STRUCTURE IN ATP-FORM'''
+==KIF1A HEAD-MICROTUBULE COMPLEX STRUCTURE IN ATP-FORM==
+<SX load='1ia0' size='340' side='right' viewer='molstar' caption='[[1ia0]], [[Resolution|resolution]] 15.00&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[1ia0]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus] and [https://en.wikipedia.org/wiki/Sus_scrofa Sus scrofa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IA0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1IA0 FirstGlance]. <br>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 15&#8491;</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACP:PHOSPHOMETHYLPHOSPHONIC+ACID+ADENYLATE+ESTER'>ACP</scene>, <scene name='pdbligand=GDP:GUANOSINE-5-DIPHOSPHATE'>GDP</scene>, <scene name='pdbligand=GTP:GUANOSINE-5-TRIPHOSPHATE'>GTP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=TXL:TAXOTERE'>TXL</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=1ia0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ia0 OCA], [https://pdbe.org/1ia0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ia0 RCSB], [https://www.ebi.ac.uk/pdbsum/1ia0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ia0 ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/TBA1A_PIG TBA1A_PIG] Tubulin is the major constituent of microtubules. It binds two moles of GTP, one at an exchangeable site on the beta chain and one at a non-exchangeable site on the alpha chain.
+== 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/ia/1ia0_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=1ia0 ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+Kinesin motors are specialized enzymes that use hydrolysis of ATP to generate force and movement along their cellular tracks, the microtubules. Although numerous biochemical and biophysical studies have accumulated much data that link microtubule-assisted ATP hydrolysis to kinesin motion, the structural view of kinesin movement remains unclear. This study of the monomeric kinesin motor KIF1A combines X-ray crystallography and cryo-electron microscopy, and allows analysis of force-generating conformational changes at atomic resolution. The motor is revealed in its two functionally critical states-complexed with ADP and with a non-hydrolysable analogue of ATP. The conformational change observed between the ADP-bound and the ATP-like structures of the KIF1A catalytic core is modular, extends to all kinesins and is similar to the conformational change used by myosin motors and G proteins. Docking of the ADP-bound and ATP-like crystallographic models of KIF1A into the corresponding cryo-electron microscopy maps suggests a rationale for the plus-end directional bias associated with the kinesin catalytic core.
-==Overview==
+Switch-based mechanism of kinesin motors.,Kikkawa M, Sablin EP, Okada Y, Yajima H, Fletterick RJ, Hirokawa N Nature. 2001 May 24;411(6836):439-45. PMID:11373668<ref>PMID:11373668</ref>
-Kinesin motors are specialized enzymes that use hydrolysis of ATP to generate force and movement along their cellular tracks, the microtubules. Although numerous biochemical and biophysical studies have accumulated much data that link microtubule-assisted ATP hydrolysis to kinesin motion, the structural view of kinesin movement remains unclear. This study of the monomeric kinesin motor KIF1A combines X-ray crystallography and cryo-electron microscopy, and allows analysis of force-generating conformational changes at atomic resolution. The motor is revealed in its two functionally critical states-complexed with ADP and with a non-hydrolysable analogue of ATP. The conformational change observed between the ADP-bound and the ATP-like structures of the KIF1A catalytic core is modular, extends to all kinesins and is similar to the conformational change used by myosin motors and G proteins. Docking of the ADP-bound and ATP-like crystallographic models of KIF1A into the corresponding cryo-electron microscopy maps suggests a rationale for the plus-end directional bias associated with the kinesin catalytic core.
-==About this Structure==
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-IA0 is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus] and [http://en.wikipedia.org/wiki/Sus_scrofa Sus scrofa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IA0 OCA].
+</div>
+<div class="pdbe-citations 1ia0" style="background-color:#fffaf0;"></div>
-==Reference==
+==See Also==
-Switch-based mechanism of kinesin motors., Kikkawa M, Sablin EP, Okada Y, Yajima H, Fletterick RJ, Hirokawa N, Nature. 2001 May 24;411(6836):439-45. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11373668 11373668]
+*[[Kinesin 3D Structures|Kinesin 3D Structures]]
+*[[Tubulin 3D Structures|Tubulin 3D Structures]]
+== References ==
+<references/>
+__TOC__
+</SX>
+[[Category: Large Structures]]
 [[Category: Mus musculus]]
-[[Category: Protein complex]]
 [[Category: Sus scrofa]]
-[[Category: Fletterick, R J.]]
+[[Category: Fletterick RJ]]
-[[Category: Hirokawa, N.]]
+[[Category: Hirokawa N]]
-[[Category: Kikkawa, M.]]
+[[Category: Kikkawa M]]
-[[Category: Okada, Y.]]
+[[Category: Okada Y]]
-[[Category: Sablin, E P.]]
+[[Category: Sablin EP]]
-[[Category: Yajima, H.]]
+[[Category: Yajima H]]
-[[Category: Cryo-electron microscopy]]
-[[Category: Fitting of x-ray structures into cryo-em reconstruction]]
-[[Category: Kif1a]]
-[[Category: Microtubule]]
-[[Category: Tubulin]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 19:45:25 2008''