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Comment
. 2011 Mar 4;331(6021):1143-4.
doi: 10.1126/science.1203978.

Biochemistry. Molecular motors, beauty in complexity

James A Spudich  1
Affiliations
Comment

Biochemistry. Molecular motors, beauty in complexity

James A Spudich. Science. .
No abstract available

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Figures

Figure
Figure. Structure of the dynein motor
Dynein is depicted bound to a microtubule next to the motor domain of kinesin 1. The six AAA domains (dark blue, light blue, green, yellow, orange, and red), linker (purple), buttress, and stalk are indicated. The affinity of the microtubule binding domain is modulated by transitions in the ATPase cycle, primarily by the AAA1 ATPase domain (dark blue). In Carter et al.’s crystal structure, the stalk was truncated just below the point at which the buttress meets the stalk. The structure of the distal microtubule binding domain is from (12), and an intervening coiled coil of the proper length is introduced in this figure.
See this image and copyright information in PMC

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References

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    1. Rayment I, et al. Science. 1993;261:5117. - PubMed
    1. Carter AP, et al. Science. 2011;331:1159. - PMC - PubMed
    1. Gibbons IR, Rowe AJ. Science. 1965;149:424. - PubMed
    1. Paschal BM, Shpetner HS, Vallee RB. J. Cell Biol. 1987;105:1273. - PMC - PubMed

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