1ii6: Difference between revisions
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[[Image:1ii6.gif|left|200px]] | [[Image:1ii6.gif|left|200px]] | ||
'''Crystal Structure of the Mitotic Kinesin Eg5 in Complex with Mg-ADP.''' | {{Structure | ||
|PDB= 1ii6 |SIZE=350|CAPTION= <scene name='initialview01'>1ii6</scene>, resolution 2.1Å | |||
|SITE= | |||
|LIGAND= <scene name='pdbligand=NO3:NITRATE+ION'>NO3</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene> and <scene name='pdbligand=ADP:ADENOSINE-5'-DIPHOSPHATE'>ADP</scene> | |||
|ACTIVITY= | |||
|GENE= Eg5 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]) | |||
}} | |||
'''Crystal Structure of the Mitotic Kinesin Eg5 in Complex with Mg-ADP.''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1II6 is a [ | 1II6 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1II6 OCA]. | ||
==Reference== | ==Reference== | ||
Crystal structure of the mitotic spindle kinesin Eg5 reveals a novel conformation of the neck-linker., Turner J, Anderson R, Guo J, Beraud C, Fletterick R, Sakowicz R, J Biol Chem. 2001 Jul 6;276(27):25496-502. Epub 2001 Apr 27. PMID:[http:// | Crystal structure of the mitotic spindle kinesin Eg5 reveals a novel conformation of the neck-linker., Turner J, Anderson R, Guo J, Beraud C, Fletterick R, Sakowicz R, J Biol Chem. 2001 Jul 6;276(27):25496-502. Epub 2001 Apr 27. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11328809 11328809] | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: mg-adp complex]] | [[Category: mg-adp complex]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:50:41 2008'' | ||
Revision as of 12:50, 20 March 2008
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| , resolution 2.1Å | |||||||
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| Ligands: | , and | ||||||
| Gene: | Eg5 (Homo sapiens) | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystal Structure of the Mitotic Kinesin Eg5 in Complex with Mg-ADP.
OverviewOverview
Success of mitosis depends upon the coordinated and regulated activity of many cellular factors, including kinesin motor proteins, which are required for the assembly and function of the mitotic spindle. Eg5 is a kinesin implicated in the formation of the bipolar spindle and its movement prior to and during anaphase. We have determined the crystal structure of the Eg5 motor domain with ADP-Mg bound. This structure revealed a new intramolecular binding site of the neck-linker. In other kinesins, the neck-linker has been shown to be a critical mechanical element for force generation. The neck-linker of conventional kinesin is believed to undergo an ordered-to-disordered transition as it translocates along a microtubule. The structure of Eg5 showed an ordered neck-linker conformation in a position never observed previously. The docking of the neck-linker relies upon residues conserved only in the Eg5 subfamily of kinesin motors. Based on this new information, we suggest that the neck-linker of Eg5 may undergo an ordered-to-ordered transition during force production. This ratchet-like mechanism is consistent with the biological activity of Eg5.
About this StructureAbout this Structure
1II6 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
ReferenceReference
Crystal structure of the mitotic spindle kinesin Eg5 reveals a novel conformation of the neck-linker., Turner J, Anderson R, Guo J, Beraud C, Fletterick R, Sakowicz R, J Biol Chem. 2001 Jul 6;276(27):25496-502. Epub 2001 Apr 27. PMID:11328809
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