1vfv: Difference between revisions

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-[[Image:1vfv.gif|left|200px]]
- {{Structure
+==Crystal Structure of the Kif1A Motor Domain Complexed With Mg-AMPPNP==
-|PDB= 1vfv |SIZE=350|CAPTION= <scene name='initialview01'>1vfv</scene>, resolution 1.85&Aring;
+<StructureSection load='1vfv' size='340' side='right'caption='[[1vfv]], [[Resolution|resolution]] 1.85&Aring;' scene=''>
-|SITE=
+== Structural highlights ==
-|LIGAND= <scene name='pdbligand=ANP:PHOSPHOAMINOPHOSPHONIC+ACID-ADENYLATE+ESTER'>ANP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>
+<table><tr><td colspan='2'>[[1vfv]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1VFV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1VFV FirstGlance]. <br>
-|ACTIVITY=
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.85&#8491;</td></tr>
-|GENE=
+<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=MG:MAGNESIUM+ION'>MG</scene></td></tr>
-|DOMAIN=
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1vfv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1vfv OCA], [https://pdbe.org/1vfv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1vfv RCSB], [https://www.ebi.ac.uk/pdbsum/1vfv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1vfv ProSAT]</span></td></tr>
-|RELATEDENTRY=[[1vfw|1VFW]], [[1vfx|1VFX]], [[1vfz|1VFZ]]
+</table>
-|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1vfv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1vfv OCA], [http://www.ebi.ac.uk/pdbsum/1vfv PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1vfv RCSB]</span>
+== Function ==
-}}
+[https://www.uniprot.org/uniprot/KIF1A_MOUSE KIF1A_MOUSE] Motor for anterograde axonal transport of synaptic vesicle precursors.
+== 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/vf/1vfv_consurf.spt"</scriptWhenChecked>
+    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.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=1vfv ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+The motor protein kinesin moves along microtubules, driven by adenosine triphosphate (ATP) hydrolysis. However, it remains unclear how kinesin converts the chemical energy into mechanical movement. We report crystal structures of monomeric kinesin KIF1A with three transition-state analogs: adenylyl imidodiphosphate (AMP-PNP), adenosine diphosphate (ADP)-vanadate, and ADP-AlFx (aluminofluoride complexes). These structures, together with known structures of the ADP-bound state and the adenylyl-(beta,gamma-methylene) diphosphate (AMP-PCP)-bound state, show that kinesin uses two microtubule-binding loops in an alternating manner to change its interaction with microtubules during the ATP hydrolysis cycle; loop L11 is extended in the AMP-PNP structure, whereas loop L12 is extended in the ADP structure. ADP-vanadate displays an intermediate structure in which a conformational change in two switch regions causes both loops to be raised from the microtubule, thus actively detaching kinesin.
-'''Crystal Structure of the Kif1A Motor Domain Complexed With Mg-AMPPNP'''
+KIF1A alternately uses two loops to bind microtubules.,Nitta R, Kikkawa M, Okada Y, Hirokawa N Science. 2004 Jul 30;305(5684):678-83. PMID:15286375<ref>PMID:15286375</ref>
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
+<div class="pdbe-citations 1vfv" style="background-color:#fffaf0;"></div>
-==Overview==
+==See Also==
-The motor protein kinesin moves along microtubules, driven by adenosine triphosphate (ATP) hydrolysis. However, it remains unclear how kinesin converts the chemical energy into mechanical movement. We report crystal structures of monomeric kinesin KIF1A with three transition-state analogs: adenylyl imidodiphosphate (AMP-PNP), adenosine diphosphate (ADP)-vanadate, and ADP-AlFx (aluminofluoride complexes). These structures, together with known structures of the ADP-bound state and the adenylyl-(beta,gamma-methylene) diphosphate (AMP-PCP)-bound state, show that kinesin uses two microtubule-binding loops in an alternating manner to change its interaction with microtubules during the ATP hydrolysis cycle; loop L11 is extended in the AMP-PNP structure, whereas loop L12 is extended in the ADP structure. ADP-vanadate displays an intermediate structure in which a conformational change in two switch regions causes both loops to be raised from the microtubule, thus actively detaching kinesin.
+*[[Kinesin 3D Structures|Kinesin 3D Structures]]
+== References ==
-==About this Structure==
+<references/>
-VFV is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1VFV OCA].
+__TOC__
+</StructureSection>
-==Reference==
+[[Category: Large Structures]]
-KIF1A alternately uses two loops to bind microtubules., Nitta R, Kikkawa M, Okada Y, Hirokawa N, Science. 2004 Jul 30;305(5684):678-83. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15286375 15286375]
 [[Category: Mus musculus]]
-[[Category: Single protein]]
+[[Category: Hirokawa N]]
-[[Category: Hirokawa, N.]]
+[[Category: Kikkawa M]]
-[[Category: Kikkawa, M.]]
+[[Category: Nitta R]]
-[[Category: Nitta, R.]]
+[[Category: Okada Y]]
-[[Category: Okada, Y.]]
-[[Category: kinesin]]
-[[Category: microtubule]]
-[[Category: motor]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 00:23:48 2008''