KIF1A alternately uses two loops to bind microtubules

Science

Volumn 305, Issue 5684, 2004, Pages 678-683

  Nitta, Ryo ^a   Kikkawa, Masahide ^a,b   Okada, Yasushi ^a   Hirokawa, Nobutaka ^a  

^a UNIVERSITY OF TOKYO   (Japan)

^b UNIVERSITY OF TEXAS SOUTHWESTERN MEDICAL CENTER   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINETRIPHOSPHATE; CRYSTAL STRUCTURE; HYDROLYSIS;

CHEMICAL ENERGY; MECHANICAL MOVEMENT; MICROTUBULES;

PROTEINS;

ADENOSINE DIPHOSPHATE; ADENOSINE TRIPHOSPHATE; ADENYLYLIMIDODIPHOSPHATE; ALUMINUM FLUORIDE; BETA,GAMMA METHYLENEADENOSINE TRIPHOSPHATE; KINESIN; MYOSIN; PROTEIN KIF1A; UNCLASSIFIED DRUG; VANADIC ACID; ALUMINUM; FLUORIDE; KIF1A PROTEIN, MOUSE; NERVE PROTEIN; PHOSPHATE;

BIOLOGY;

ARTICLE; BINDING AFFINITY; CONFORMATIONAL TRANSITION; CRYSTAL STRUCTURE; DISSOCIATION CONSTANT; HYDROLYSIS; MICROTUBULE; PRIORITY JOURNAL; PROTEIN STRUCTURE; TRANSMISSION ELECTRON MICROSCOPY; ANIMAL; BINDING SITE; CHEMICAL STRUCTURE; CHEMISTRY; HYDROGEN BOND; METABOLISM; MOUSE; PROTEIN CONFORMATION; PROTEIN SECONDARY STRUCTURE; PROTEIN TERTIARY STRUCTURE; X RAY CRYSTALLOGRAPHY;

ADENOSINE TRIPHOSPHATE; ADENYLYL IMIDODIPHOSPHATE; ALUMINUM; ANIMALS; BINDING SITES; CRYSTALLOGRAPHY, X-RAY; FLUORIDES; HYDROGEN BONDING; KINESIN; MICE; MICROTUBULES; MODELS, MOLECULAR; NERVE TISSUE PROTEINS; PHOSPHATES; PROTEIN CONFORMATION; PROTEIN STRUCTURE, SECONDARY; PROTEIN STRUCTURE, TERTIARY; VANADATES;

EID: 3442876110     PISSN: 00368075     EISSN: None     Source Type: Journal    
DOI: 10.1126/science.1096621     Document Type: Article

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26. 216 only reflects an artificial coordination of the solvent ion in crystal can be excluded by the following reasons. First, the position of vanadate is analogous to that in myosin. With myosin, vanadate is found on the corresponding back-door residue through which the produced phosphate is thought to be released. Second, vanadate is located at the same or similar position even in solution. The position of vanadate in solution was determined by the photo cleavage experiment. With myosins, the cleavage site (P-loop) agrees well with its ADP-Vi structure (40). Similarly, KIF1A was cleaved at Loop L11, as expected from our ADP-Vi structure. This confirms that our ADP-Vi structure actually reflects the solution structure.
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47. We thank D. R. Tomchick, N. Ota, S. Wakatsuki, N. Igarashi, H. Sawa, Y. Wakabayashi, and their colleagues for technical suggestions; H. Fukuda, H. Sato, and M. Sugaya for technical and secretarial assistance; and H. Miki, M. Kawagishi, H. Yajima, T. Ogawa, E. Nitta, and our colleagues for discussions and technical assistance. Supported by a Center of Excellence Grant-in-Aid from the Ministry of Education, Culture, Sports, Science and Technology of Japan (N.H.). Coordinates for the four new structures of KIF1A have been deposited in the PDB database and are available under the following accession codes: both 1VFV and 1VFW for the AMP-PNP form, 1VFX for the ADP-AIFx form, and 1VFZ for the ADP-Vi form.