2hxf

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{{Seed}}
 
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[[Image:2hxf.png|left|200px]]
 
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==KIF1A head-microtubule complex structure in amppnp-form==
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The line below this paragraph, containing "STRUCTURE_2hxf", creates the "Structure Box" on the page.
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<SX load='2hxf' size='340' side='right' viewer='molstar' caption='[[2hxf]], [[Resolution|resolution]] 10.00&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[2hxf]] 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=2HXF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2HXF FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 10&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ANP:PHOSPHOAMINOPHOSPHONIC+ACID-ADENYLATE+ESTER'>ANP</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=TA1:TAXOL'>TA1</scene></td></tr>
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{{STRUCTURE_2hxf| PDB=2hxf | SCENE= }}
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2hxf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2hxf OCA], [https://pdbe.org/2hxf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2hxf RCSB], [https://www.ebi.ac.uk/pdbsum/2hxf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2hxf ProSAT]</span></td></tr>
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</table>
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== Function ==
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[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.
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/hx/2hxf_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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=2hxf ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Kinesin is an ATP-driven microtubule (MT)-based motor fundamental to organelle transport. Although a number of kinesin crystal structures have been solved, the structural evidence for coupling between the bound nucleotide and the conformation of kinesin is elusive. In addition, the structural basis of the MT-induced ATPase activity of kinesin is not clear because of the absence of the MT in the structure. Here, we report cryo-electron microscopy structures of the monomeric kinesin KIF1A-MT complex in two nucleotide states at about 10 A resolution, sufficient to reveal the secondary structure. These high-resolution maps visualized clear structural changes that suggest a mechanical pathway from the nucleotide to the neck linker via the motor core rotation. In addition, new nucleotide binding pocket conformations are observed that are different from X-ray crystallographic structures; it is closed in the 5'-adenylyl-imidodiphosphate state, but open in the ADP state. These results suggest a structural model of biased diffusion movement of monomeric kinesin motor.
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===KIF1A head-microtubule complex structure in amppnp-form===
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High-resolution cryo-EM maps show the nucleotide binding pocket of KIF1A in open and closed conformations.,Kikkawa M, Hirokawa N EMBO J. 2006 Sep 20;25(18):4187-94. Epub 2006 Aug 31. PMID:16946706<ref>PMID:16946706</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 2hxf" style="background-color:#fffaf0;"></div>
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==See Also==
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The line below this paragraph, {{ABSTRACT_PUBMED_16946706}}, adds the Publication Abstract to the page
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*[[Kinesin 3D Structures|Kinesin 3D Structures]]
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(as it appears on PubMed at http://www.pubmed.gov), where 16946706 is the PubMed ID number.
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*[[Tubulin 3D Structures|Tubulin 3D Structures]]
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== References ==
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{{ABSTRACT_PUBMED_16946706}}
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<references/>
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__TOC__
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==About this Structure==
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</SX>
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2HXF 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=2HXF OCA].
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[[Category: Large Structures]]
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==Reference==
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High-resolution cryo-EM maps show the nucleotide binding pocket of KIF1A in open and closed conformations., Kikkawa M, Hirokawa N, EMBO J. 2006 Sep 20;25(18):4187-94. Epub 2006 Aug 31. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16946706 16946706]
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[[Category: Mus musculus]]
[[Category: Mus musculus]]
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[[Category: Protein complex]]
 
[[Category: Sus scrofa]]
[[Category: Sus scrofa]]
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[[Category: Hirokawa, N.]]
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[[Category: Hirokawa N]]
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[[Category: Kikkawa, M.]]
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[[Category: Kikkawa M]]
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[[Category: Microtubule-based motor]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 20:18:26 2008''
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Current revision

KIF1A head-microtubule complex structure in amppnp-form

2hxf, resolution 10.00Å

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OCA

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