1ia0: Difference between revisions

Revision as of 14:09, 21 February 2008

KIF1A HEAD-MICROTUBULE COMPLEX STRUCTURE IN ATP-FORM

OverviewOverview

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 StructureAbout this Structure

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

ReferenceReference

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

Page seeded by OCA on Thu Feb 21 13:09:34 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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-[[Image:1ia0.gif|left|200px]]<br /><applet load="1ia0" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:1ia0.gif|left|200px]]<br /><applet load="1ia0" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="1ia0, resolution 15.&Aring;" />
 '''KIF1A HEAD-MICROTUBULE COMPLEX STRUCTURE IN ATP-FORM'''<br />
 ==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.
+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==
-IA0 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 MG, GTP, GDP, TXL and ACP as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1IA0 OCA].
+IA0 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].
 ==Reference==
@@ Line 14: / Line 14: @@
 [[Category: Protein complex]]
 [[Category: Sus scrofa]]
-[[Category: Fletterick, R.J.]]
+[[Category: Fletterick, R J.]]
 [[Category: Hirokawa, N.]]
 [[Category: Kikkawa, M.]]
 [[Category: Okada, Y.]]
-[[Category: Sablin, E.P.]]
+[[Category: Sablin, E P.]]
 [[Category: Yajima, H.]]
 [[Category: ACP]]
@@ Line 31: / Line 31: @@
 [[Category: tubulin]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 17:12:22 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:09:34 2008''