1ia0: Difference between revisions
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|PDB= 1ia0 |SIZE=350|CAPTION= <scene name='initialview01'>1ia0</scene>, resolution 15.Å | |PDB= 1ia0 |SIZE=350|CAPTION= <scene name='initialview01'>1ia0</scene>, resolution 15.Å | ||
|SITE= | |SITE= | ||
|LIGAND= <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=GTP:GUANOSINE-5 | |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> | ||
|ACTIVITY= | |ACTIVITY= | ||
|GENE= KIF1A ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 Mus musculus]) | |GENE= KIF1A ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 Mus musculus]) | ||
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[[Category: tubulin]] | [[Category: tubulin]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 23 12:11:34 2008'' | ||
Revision as of 13:11, 23 March 2008
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| , resolution 15.Å | |||||||
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| Ligands: | , , , and | ||||||
| Gene: | KIF1A (Mus musculus) | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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. 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
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