Title of article :
A Common Mechanism for Microtubule Destabilizers-M Type Kinesins Stabilize Curling of the Protofilament Using the Class-Specific Neck and Loops
Author/Authors :
Okada، Yasushi نويسنده , , Hirokawa، Nobutaka نويسنده , , Ogawa، Tadayuki نويسنده , , Nitta، Ryo نويسنده ,
Issue Information :
هفته نامه با شماره پیاپی سال 2004
Pages :
-590
From page :
591
To page :
0
Abstract :
Unlike other kinesins, middle motor domain-type kinesins depolymerize the microtubule from its ends. To elucidate its mechanism, we solved the X-ray crystallographic structure of KIF2C, a murine member of this family. Three major classspecific features were identified. The class-specific N-terminal neck adopts a long and rigid helical structure extending out vertically into the interprotofilament groove. This structure explains its dual roles in targeting to the end of the microtubule and in destabilization of the lateral interaction of the protofilament. The loop L2 forms a unique finger-like structure, long and rigid enough to reach the next tubulin subunit to stabilize the peeling of the protofilament. The open conformation of the switch I loop could be reversed by the shift of the microtubule binding L8 loop, suggesting its role as the sensor to trigger ATP hydrolysis. Mutational analysis supports these structural implications.
Keywords :
NOx storage/reduction catalysts , NOx release , Emissions , NOx storage , Catalyst , NO oxidation
Journal title :
CELL
Serial Year :
2004
Journal title :
CELL
Record number :
102477
Link To Document :
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