2owm: Difference between revisions
No edit summary |
No edit summary |
||
| Line 4: | Line 4: | ||
|PDB= 2owm |SIZE=350|CAPTION= <scene name='initialview01'>2owm</scene>, resolution 3.25Å | |PDB= 2owm |SIZE=350|CAPTION= <scene name='initialview01'>2owm</scene>, resolution 3.25Å | ||
|SITE= <scene name='pdbsite=AC1:Mg+Binding+Site+For+Residue+A+1001'>AC1</scene>, <scene name='pdbsite=AC2:Mg+Binding+Site+For+Residue+B+1001'>AC2</scene>, <scene name='pdbsite=AC3:Mg+Binding+Site+For+Residue+C+1001'>AC3</scene>, <scene name='pdbsite=AC4:Mg+Binding+Site+For+Residue+D+1001'>AC4</scene>, <scene name='pdbsite=AC5:Adp+Binding+Site+For+Residue+A+1002'>AC5</scene>, <scene name='pdbsite=AC6:Adp+Binding+Site+For+Residue+B+1002'>AC6</scene>, <scene name='pdbsite=AC7:Adp+Binding+Site+For+Residue+C+1002'>AC7</scene> and <scene name='pdbsite=AC8:Adp+Binding+Site+For+Residue+D+1002'>AC8</scene> | |SITE= <scene name='pdbsite=AC1:Mg+Binding+Site+For+Residue+A+1001'>AC1</scene>, <scene name='pdbsite=AC2:Mg+Binding+Site+For+Residue+B+1001'>AC2</scene>, <scene name='pdbsite=AC3:Mg+Binding+Site+For+Residue+C+1001'>AC3</scene>, <scene name='pdbsite=AC4:Mg+Binding+Site+For+Residue+D+1001'>AC4</scene>, <scene name='pdbsite=AC5:Adp+Binding+Site+For+Residue+A+1002'>AC5</scene>, <scene name='pdbsite=AC6:Adp+Binding+Site+For+Residue+B+1002'>AC6</scene>, <scene name='pdbsite=AC7:Adp+Binding+Site+For+Residue+C+1002'>AC7</scene> and <scene name='pdbsite=AC8:Adp+Binding+Site+For+Residue+D+1002'>AC8</scene> | ||
|LIGAND= <scene name='pdbligand= | |LIGAND= <scene name='pdbligand=ADP:ADENOSINE-5'-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene> | ||
|ACTIVITY= [http://en.wikipedia.org/wiki/Plus-end-directed_kinesin_ATPase Plus-end-directed kinesin ATPase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.6.4.4 3.6.4.4] | |ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Plus-end-directed_kinesin_ATPase Plus-end-directed kinesin ATPase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.6.4.4 3.6.4.4] </span> | ||
|GENE= 17E5.250 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=5141 Neurospora crassa]) | |GENE= 17E5.250 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=5141 Neurospora crassa]) | ||
|DOMAIN= | |||
|RELATEDENTRY= | |||
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2owm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2owm OCA], [http://www.ebi.ac.uk/pdbsum/2owm PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2owm RCSB]</span> | |||
}} | }} | ||
| Line 28: | Line 31: | ||
[[Category: Muller, J.]] | [[Category: Muller, J.]] | ||
[[Category: Woehlke, G.]] | [[Category: Woehlke, G.]] | ||
[[Category: adp]] | [[Category: adp]] | ||
[[Category: kinesin]] | [[Category: kinesin]] | ||
| Line 37: | Line 38: | ||
[[Category: neck linker]] | [[Category: neck linker]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 04:24:15 2008'' | ||
Revision as of 04:24, 31 March 2008
| |||||||
| , resolution 3.25Å | |||||||
|---|---|---|---|---|---|---|---|
| Sites: | , , , , , , and | ||||||
| Ligands: | , | ||||||
| Gene: | 17E5.250 (Neurospora crassa) | ||||||
| Activity: | Plus-end-directed kinesin ATPase, with EC number 3.6.4.4 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Motor domain of Neurospora crassa kinesin-3 (NcKin3)
OverviewOverview
Neurospora crassa kinesin NcKin3 belongs to a unique fungal-specific subgroup of small Kinesin-3-related motor proteins. One of its functions appears to be the transport of mitochondria along microtubules. Here, we present the X-ray structure of a C-terminally truncated monomeric construct of NcKin3 comprising the motor domain and the neck linker, and a 3-D image reconstruction of this motor domain bound to microtubules, by cryoelectron microscopy. The protein contains Mg.ADP bound to the active site, yet the structure resembles an ATP-bound state. By comparison with structures of the Kinesin-3 motor Kif1A in different nucleotide states (Kikkawa, M. et al. (2001) Nature (London, U.K.) 411, 439-445), the NcKin3 structure corresponds to the AMPPCP complex of Kif1A rather than the AMPPNP complex. NcKin3-specific differences in the coordination of the nucleotide and asymmetric interactions between adjacent molecules in the crystal are discussed in the context of the unusual kinetics of the dimeric wild-type motor and the monomeric construct used for crystal structure analysis. The NcKin3 motor decorates microtubules at a stoichiometry of one head per alphabeta-tubulin heterodimer, thereby forming an axial periodicity of 8 nm. In spite of unusual extensions at the N-terminus and within flexible loops L2, L8a, and L12 (corresponding to the K-loop of monomeric kinesins), the microtubule binding geometry is similar to that of other members of the kinesin family.
About this StructureAbout this Structure
2OWM is a Single protein structure of sequence from Neurospora crassa. Full crystallographic information is available from OCA.
ReferenceReference
X-ray Structure and Microtubule Interaction of the Motor Domain of Neurospora crassa NcKin3, a Kinesin with Unusual Processivity(,)., Marx A, Muller J, Mandelkow EM, Woehlke G, Bouchet-Marquis C, Hoenger A, Mandelkow E, Biochemistry. 2008 Feb 19;47(7):1848-1861. Epub 2008 Jan 19. PMID:18205396
Page seeded by OCA on Mon Mar 31 04:24:15 2008