1ry6

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(New page: 200px<br /><applet load="1ry6" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ry6, resolution 1.60&Aring;" /> '''Crystal Structure of...)
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caption="1ry6, resolution 1.60&Aring;" />
'''Crystal Structure of Internal Kinesin Motor Domain'''<br />
'''Crystal Structure of Internal Kinesin Motor Domain'''<br />
==Overview==
==Overview==
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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.
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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 Structure==
==About this Structure==
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1RY6 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Plasmodium_falciparum Plasmodium falciparum] with SO4 as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1RY6 OCA].
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1RY6 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Plasmodium_falciparum Plasmodium falciparum] with <scene name='pdbligand=SO4:'>SO4</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1RY6 OCA].
==Reference==
==Reference==
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[[Category: nucleotide-free]]
[[Category: nucleotide-free]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Sat Nov 24 23:30:15 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:55:53 2008''

Revision as of 12:55, 21 February 2008


1ry6, resolution 1.60Å

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Crystal Structure of Internal Kinesin Motor Domain

Overview

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 Structure

1RY6 is a Single protein structure of sequence from Plasmodium falciparum with as ligand. Full crystallographic information is available from OCA.

Reference

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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