1ry6: Difference between revisions
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|PDB= 1ry6 |SIZE=350|CAPTION= <scene name='initialview01'>1ry6</scene>, resolution 1.60Å | |PDB= 1ry6 |SIZE=350|CAPTION= <scene name='initialview01'>1ry6</scene>, resolution 1.60Å | ||
|SITE= | |SITE= | ||
|LIGAND= <scene name='pdbligand=SO4:SULFATE ION'>SO4</scene> | |LIGAND= <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene> | ||
|ACTIVITY= | |ACTIVITY= | ||
|GENE= PFL2165W ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=5833 Plasmodium falciparum]) | |GENE= PFL2165W ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=5833 Plasmodium falciparum]) | ||
|DOMAIN= | |||
|RELATEDENTRY= | |||
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ry6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ry6 OCA], [http://www.ebi.ac.uk/pdbsum/1ry6 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1ry6 RCSB]</span> | |||
}} | }} | ||
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[[Category: Shipley, K.]] | [[Category: Shipley, K.]] | ||
[[Category: Turner, J.]] | [[Category: Turner, J.]] | ||
[[Category: kinesin motor domain]] | [[Category: kinesin motor domain]] | ||
[[Category: nucleotide-free]] | [[Category: nucleotide-free]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 23:34:39 2008'' | ||
Revision as of 23:34, 30 March 2008
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| , resolution 1.60Å | |||||||
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| Ligands: | |||||||
| Gene: | PFL2165W (Plasmodium falciparum) | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystal Structure of Internal Kinesin Motor Domain
OverviewOverview
With their ability to depolymerize microtubules (MTs), KinI kinesins are the rogue members of the kinesin family. Here we present the 1.6 A crystal structure of a KinI motor core from Plasmodium falciparum, which is sufficient for depolymerization in vitro. Unlike all published kinesin structures to date, nucleotide is not present, and there are noticeable differences in loop regions L6 and L10 (the plus-end tip), L2 and L8 and in switch II (L11 and helix4); otherwise, the pKinI structure is very similar to previous kinesin structures. KinI-conserved amino acids were mutated to alanine, and studied for their effects on depolymerization and ATP hydrolysis. Notably, mutation of three residues in L2 appears to primarily affect depolymerization, rather than general MT binding or ATP hydrolysis. The results of this study confirm the suspected importance of loop 2 for KinI function, and provide evidence that KinI is specialized to hydrolyze ATP after initiating depolymerization.
About this StructureAbout this Structure
1RY6 is a Single protein structure of sequence from Plasmodium falciparum. Full crystallographic information is available from OCA.
ReferenceReference
Structure of a kinesin microtubule depolymerization machine., Shipley K, Hekmat-Nejad M, Turner J, Moores C, Anderson R, Milligan R, Sakowicz R, Fletterick R, EMBO J. 2004 Apr 7;23(7):1422-32. Epub 2004 Mar 18. PMID:15029249
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