1i5s
From Proteopedia
| Line 4: | Line 4: | ||
|PDB= 1i5s |SIZE=350|CAPTION= <scene name='initialview01'>1i5s</scene>, resolution 2.20Å | |PDB= 1i5s |SIZE=350|CAPTION= <scene name='initialview01'>1i5s</scene>, resolution 2.20Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand= | + | |LIGAND= <scene name='pdbligand=ADP:ADENOSINE-5'-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= KIFA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 Mus musculus]) | |GENE= KIFA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 Mus musculus]) | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1i5s FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1i5s OCA], [http://www.ebi.ac.uk/pdbsum/1i5s PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1i5s RCSB]</span> | ||
}} | }} | ||
| Line 28: | Line 31: | ||
[[Category: Sablin, E P.]] | [[Category: Sablin, E P.]] | ||
[[Category: Yajima, H.]] | [[Category: Yajima, H.]] | ||
| - | [[Category: ADP]] | ||
| - | [[Category: MG]] | ||
[[Category: kinesin catalytic core]] | [[Category: kinesin catalytic core]] | ||
[[Category: motor domain]] | [[Category: motor domain]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:15:00 2008'' |
Revision as of 18:15, 30 March 2008
| |||||||
| , resolution 2.20Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , | ||||||
| Gene: | KIFA (Mus musculus) | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
CRYSTAL STRUCTURE OF THE KIF1A MOTOR DOMAIN COMPLEXED WITH MG-ADP
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
1I5S is a Single protein structure of sequence from Mus musculus. 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
Page seeded by OCA on Sun Mar 30 21:15:00 2008
