2bkh: Difference between revisions
No edit summary |
No edit summary |
||
| Line 4: | Line 4: | ||
|PDB= 2bkh |SIZE=350|CAPTION= <scene name='initialview01'>2bkh</scene>, resolution 2.40Å | |PDB= 2bkh |SIZE=350|CAPTION= <scene name='initialview01'>2bkh</scene>, resolution 2.40Å | ||
|SITE= <scene name='pdbsite=AC1:Gol+Binding+Site+For+Chain+A'>AC1</scene> | |SITE= <scene name='pdbsite=AC1:Gol+Binding+Site+For+Chain+A'>AC1</scene> | ||
|LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene> | |LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene> | ||
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
|DOMAIN= | |||
|RELATEDENTRY= | |||
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2bkh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2bkh OCA], [http://www.ebi.ac.uk/pdbsum/2bkh PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2bkh RCSB]</span> | |||
}} | }} | ||
| Line 30: | Line 33: | ||
[[Category: Wells, A.]] | [[Category: Wells, A.]] | ||
[[Category: Yengo, C.]] | [[Category: Yengo, C.]] | ||
[[Category: calmodulin]] | [[Category: calmodulin]] | ||
[[Category: muscle protein]] | [[Category: muscle protein]] | ||
| Line 39: | Line 40: | ||
[[Category: reverse myosin]] | [[Category: reverse myosin]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 02:07:43 2008'' | ||
Revision as of 23:07, 30 March 2008
| |||||||||||||
| 2bkh, resolution 2.40Å | |||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Sites: | AC1 | ||||||||||||
| Ligands: | CA, GOL | ||||||||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||||||
MYOSIN VI NUCLEOTIDE-FREE (MDINSERT2) CRYSTAL STRUCTURE
Overview
Here we solve a 2.4-A structure of a truncated version of the reverse-direction myosin motor, myosin VI, that contains the motor domain and binding sites for two calmodulin molecules. The structure reveals only minor differences in the motor domain from that in plus-end directed myosins, with the exception of two unique inserts. The first is near the nucleotide-binding pocket and alters the rates of nucleotide association and dissociation. The second unique insert forms an integral part of the myosin VI converter domain along with a calmodulin bound to a novel target motif within the insert. This serves to redirect the effective 'lever arm' of myosin VI, which includes a second calmodulin bound to an 'IQ motif', towards the pointed (minus) end of the actin filament. This repositioning largely accounts for the reverse directionality of this class of myosin motors. We propose a model incorporating a kinesin-like uncoupling/docking mechanism to provide a full explanation of the movements of myosin VI.
About this Structure
2BKH is a Protein complex structure of sequences from Drosophila melanogaster and Sus scrofa. Full crystallographic information is available from OCA.
Reference
The structure of the myosin VI motor reveals the mechanism of directionality reversal., Menetrey J, Bahloul A, Wells AL, Yengo CM, Morris CA, Sweeney HL, Houdusse A, Nature. 2005 Jun 9;435(7043):779-85. PMID:15944696
Page seeded by OCA on Mon Mar 31 02:07:43 2008
