1GOJ

Structure of a fast kinesin: Implications for ATPase mechanism and interactions with microtubules

1GOJ の概要

• エントリーDOI: 10.2210/pdb1goj/pdb
• 分子名称: KINESIN HEAVY CHAIN, ADENOSINE-5'-DIPHOSPHATE, MAGNESIUM ION, ... (4 entities in total)
• 機能のキーワード: kinesin, motor protein, atpase, neurospora crassa
• 由来する生物種: NEUROSPORA CRASSA
• 細胞内の位置: Cytoplasm, cytoskeleton (Probable): P48467
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 39244.34

構造登録者

Song, Y.-H.,Marx, A.,Muller, J.,Woehlke, G.,Schliwa, M.,Krebs, A.,Hoenger, A.,Mandelkow, E. (登録日: 2001-10-21, 公開日: 2001-11-30, 最終更新日: 2023-12-13)

主引用文献

Song, Y.-H.,Marx, A.,Muller, J.,Woehlke, G.,Schliwa, M.,Krebs, A.,Hoenger, A.,Mandelkow, E.
Structure of a Fast Kinesin: Implications for ATPase Mechanism and Interactions with Microtubules
Embo J., 20:6213-, 2001

PubMed Abstract: We determined the crystal structure of the motor domain of the fast fungal kinesin from Neurospora crassa (NcKin). The structure has several unique features. (i) Loop 11 in the switch 2 region is ordered and enables one to describe the complete nucleotide-binding pocket, including three inter-switch salt bridges between switch 1 and 2. (ii) Loop 9 in the switch 1 region bends outwards, making the nucleotide-binding pocket very wide. The displacement in switch 1 resembles that of the G-protein ras complexed with its guanosine nucleotide exchange factor. (iii) Loop 5 in the entrance to the nucleotide-binding pocket is remarkably long and interacts with the ribose of ATP. (iv) The linker and neck region is not well defined, indicating that it is mobile. (v) Image reconstructions of ice-embedded microtubules decorated with NcKin show that it interacts with several tubulin subunits, including a central beta-tubulin monomer and the two flanking alpha-tubulin monomers within the microtubule protofilament. Comparison of NcKin with other kinesins, myosin and G-proteins suggests that the rate-limiting step of ADP release is accelerated in the fungal kinesin and accounts for the unusually high velocity and ATPase activity.

PubMed: 11707393
DOI: 10.1093/EMBOJ/20.22.6213

実験手法

X-RAY DIFFRACTION (2.3 Å)