1goj
From Proteopedia
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STRUCTURE OF A FAST KINESIN: IMPLICATIONS FOR ATPASE MECHANISM AND INTERACTIONS WITH MICROTUBULES
Overview
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 ... [(full description)]
About this Structure
1GOJ is a [Single protein] structure of sequence from [Neurospora crassa] with MG and ADP as [ligands]. Active as [Plus-end-directed kinesin ATPase], with EC number [3.6.4.4]. Structure known Active Site: ADP. Full crystallographic information is available from [OCA].
Reference
Structure of a fast kinesin: implications for ATPase mechanism and interactions with microtubules., Song YH, Marx A, Muller J, Woehlke G, Schliwa M, Krebs A, Hoenger A, Mandelkow E, EMBO J. 2001 Nov 15;20(22):6213-25. PMID:11707393
Page seeded by OCA on Tue Oct 30 11:36:47 2007
Categories: Neurospora crassa | Plus-end-directed kinesin ATPase | Single protein | Hoenger, A. | Krebs, A. | Mandelkow, E. | Marx, A. | Muller, J. | Schliwa, M. | Song, Y.H. | Woehlke, G. | ADP | MG | Atpase | Kinesin | Motor protein
