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-Structure paper
タイトル | Nucleotide-induced conformations in the neck region of dimeric kinesin. |
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ジャーナル・号・ページ | EMBO J, Vol. 22, Issue 7, Page 1518-1528, Year 2003 |
掲載日 | 2003年4月1日 |
![]() | Georgios Skiniotis / Thomas Surrey / Stephan Altmann / Heinz Gross / Young-Hwa Song / Eckhard Mandelkow / Andreas Hoenger / ![]() |
PubMed 要旨 | The neck region of kinesin constitutes a key component in the enzyme's walking mechanism. Here we applied cryoelectron microscopy and image reconstruction to investigate the location of the kinesin ...The neck region of kinesin constitutes a key component in the enzyme's walking mechanism. Here we applied cryoelectron microscopy and image reconstruction to investigate the location of the kinesin neck in dimeric and monomeric constructs complexed to microtubules. To this end we enhanced the visibility of this region by engineering an SH3 domain into the transition between neck linker and neck coiled coil. The resulting chimeric kinesin constructs remained functional as verified by physiology assays. In the presence of AMP-PNP the SH3 domains allowed us to identify the position of the neck in a well defined conformation and revealed its high flexibility in the absence of nucleotide. We show here the double-headed binding of dimeric kinesin along the same protofilament, which is characterized by the opposite directionality of neck linkers. In this configuration the neck coiled coil appears fully zipped. The position of the neck region in dimeric constructs is not affected by the presence of the tubulin C-termini as confirmed by subtilisin treatment of microtubules prior to motor decoration. |
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手法 | EM (らせん対称) |
解像度 | 25.0 Å |
構造データ | ![]() EMDB-1037: ![]() EMDB-1038: ![]() EMDB-1039: ![]() EMDB-1040: ![]() EMDB-1041: |
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