1ia0

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[[Image:1ia0.gif|left|200px]]<br /><applet load="1ia0" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:1ia0.gif|left|200px]]
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caption="1ia0, resolution 15.&Aring;" />
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'''KIF1A HEAD-MICROTUBULE COMPLEX STRUCTURE IN ATP-FORM'''<br />
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{{Structure
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|PDB= 1ia0 |SIZE=350|CAPTION= <scene name='initialview01'>1ia0</scene>, resolution 15.&Aring;
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|SITE=
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|LIGAND= <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=GTP:GUANOSINE-5'-TRIPHOSPHATE'>GTP</scene>, <scene name='pdbligand=GDP:GUANOSINE-5'-DIPHOSPHATE'>GDP</scene>, <scene name='pdbligand=TXL:TAXOTERE'>TXL</scene> and <scene name='pdbligand=ACP:PHOSPHOMETHYLPHOSPHONIC ACID ADENYLATE ESTER'>ACP</scene>
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|ACTIVITY=
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|GENE= KIF1A ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 Mus musculus])
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}}
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'''KIF1A HEAD-MICROTUBULE COMPLEX STRUCTURE IN ATP-FORM'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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1IA0 is a [http://en.wikipedia.org/wiki/Protein_complex 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] with <scene name='pdbligand=MG:'>MG</scene>, <scene name='pdbligand=GTP:'>GTP</scene>, <scene name='pdbligand=GDP:'>GDP</scene>, <scene name='pdbligand=TXL:'>TXL</scene> and <scene name='pdbligand=ACP:'>ACP</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IA0 OCA].
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1IA0 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].
==Reference==
==Reference==
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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://ispc.weizmann.ac.il//pmbin/getpm?pmid=11373668 11373668]
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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]
[[Category: Mus musculus]]
[[Category: Mus musculus]]
[[Category: Protein complex]]
[[Category: Protein complex]]
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[[Category: MG]]
[[Category: MG]]
[[Category: TXL]]
[[Category: TXL]]
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[[Category: cryo-electron microscopy ]]
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[[Category: cryo-electron microscopy]]
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[[Category: fitting of x-ray structures into cryo-em reconstructions]]
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[[Category: fitting of x-ray structures into cryo-em reconstruction]]
[[Category: kif1a]]
[[Category: kif1a]]
[[Category: microtubule]]
[[Category: microtubule]]
[[Category: tubulin]]
[[Category: tubulin]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:09:34 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:47:32 2008''

Revision as of 09:47, 20 March 2008


PDB ID 1ia0

Drag the structure with the mouse to rotate
, resolution 15.Å
Ligands: , , , and
Gene: KIF1A (Mus musculus)
Coordinates: save as pdb, mmCIF, xml



KIF1A HEAD-MICROTUBULE COMPLEX STRUCTURE IN ATP-FORM


Overview

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

1IA0 is a Protein complex structure of sequences from Mus musculus and Sus scrofa. Full crystallographic information is available from OCA.

Reference

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

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