1cz7
From Proteopedia
(New page: 200px<br /><applet load="1cz7" size="450" color="white" frame="true" align="right" spinBox="true" caption="1cz7, resolution 2.9Å" /> '''THE CRYSTAL STRUCTURE...) |
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| - | [[Image:1cz7.gif|left|200px]]<br /><applet load="1cz7" size=" | + | [[Image:1cz7.gif|left|200px]]<br /><applet load="1cz7" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1cz7, resolution 2.9Å" /> | caption="1cz7, resolution 2.9Å" /> | ||
'''THE CRYSTAL STRUCTURE OF A MINUS-END DIRECTED MICROTUBULE MOTOR PROTEIN NCD REVEALS VARIABLE DIMER CONFORMATIONS'''<br /> | '''THE CRYSTAL STRUCTURE OF A MINUS-END DIRECTED MICROTUBULE MOTOR PROTEIN NCD REVEALS VARIABLE DIMER CONFORMATIONS'''<br /> | ||
==Overview== | ==Overview== | ||
| - | BACKGROUND: The kinesin superfamily of microtubule-associated motor | + | BACKGROUND: The kinesin superfamily of microtubule-associated motor proteins are important for intracellular transport and for cell division in eukaryotes. Conventional kinesins have the motor domain at the N terminus of the heavy chain and move towards the plus end of microtubules. The ncd protein is necessary for chromosome segregation in meiosis. It belongs to a subfamily of kinesins that have the motor domain at the C terminus and move towards the minus end of microtubules. RESULTS: The crystal structure of dimeric ncd has been obtained at 2.9 A resolution from crystals with the C222(1) space group, with two independent dimers per asymmetric unit. The motor domains in these dimers are not related by crystallographic symmetry and the two ncd dimers have significantly different conformations. An alpha-helical coiled coil connects, and interacts with, the motor domains. CONCLUSIONS: The ncd protein has a very compact structure, largely due to extended interactions of the coiled coil with the head domains. Despite this, we find that the overall conformation of the ncd dimer can be rotated by as much as 10 degrees away from that of the twofold-symmetric archetypal ncd. The crystal structures of conventional kinesin and of ncd suggest a structural rationale for the reversal of the direction of movement in chimeric kinesins. |
==About this Structure== | ==About this Structure== | ||
| - | 1CZ7 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Drosophila_melanogaster Drosophila melanogaster] with MG and ADP as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | + | 1CZ7 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Drosophila_melanogaster Drosophila melanogaster] with <scene name='pdbligand=MG:'>MG</scene> and <scene name='pdbligand=ADP:'>ADP</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CZ7 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Drosophila melanogaster]] | [[Category: Drosophila melanogaster]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Bonis, S | + | [[Category: Bonis, S De.]] |
[[Category: Burmeister, W.]] | [[Category: Burmeister, W.]] | ||
[[Category: Cohen-Addad, C.]] | [[Category: Cohen-Addad, C.]] | ||
| - | [[Category: Kozielski, F | + | [[Category: Kozielski, F K.]] |
[[Category: Wade, R.]] | [[Category: Wade, R.]] | ||
[[Category: ADP]] | [[Category: ADP]] | ||
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[[Category: ncd crystal structure]] | [[Category: ncd crystal structure]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:11:11 2008'' |
Revision as of 10:11, 21 February 2008
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THE CRYSTAL STRUCTURE OF A MINUS-END DIRECTED MICROTUBULE MOTOR PROTEIN NCD REVEALS VARIABLE DIMER CONFORMATIONS
Overview
BACKGROUND: The kinesin superfamily of microtubule-associated motor proteins are important for intracellular transport and for cell division in eukaryotes. Conventional kinesins have the motor domain at the N terminus of the heavy chain and move towards the plus end of microtubules. The ncd protein is necessary for chromosome segregation in meiosis. It belongs to a subfamily of kinesins that have the motor domain at the C terminus and move towards the minus end of microtubules. RESULTS: The crystal structure of dimeric ncd has been obtained at 2.9 A resolution from crystals with the C222(1) space group, with two independent dimers per asymmetric unit. The motor domains in these dimers are not related by crystallographic symmetry and the two ncd dimers have significantly different conformations. An alpha-helical coiled coil connects, and interacts with, the motor domains. CONCLUSIONS: The ncd protein has a very compact structure, largely due to extended interactions of the coiled coil with the head domains. Despite this, we find that the overall conformation of the ncd dimer can be rotated by as much as 10 degrees away from that of the twofold-symmetric archetypal ncd. The crystal structures of conventional kinesin and of ncd suggest a structural rationale for the reversal of the direction of movement in chimeric kinesins.
About this Structure
1CZ7 is a Single protein structure of sequence from Drosophila melanogaster with and as ligands. Full crystallographic information is available from OCA.
Reference
The crystal structure of the minus-end-directed microtubule motor protein ncd reveals variable dimer conformations., Kozielski F, De Bonis S, Burmeister WP, Cohen-Addad C, Wade RH, Structure. 1999 Nov 15;7(11):1407-16. PMID:10574799
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