We apologize for Proteopedia being slow to respond. For the past two years, a new implementation of Proteopedia has been being built. Soon, it will replace this 18-year old system. All existing content will be moved to the new system at a date that will be announced here.

1cz7

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1cz7.gif|left|200px]]<br /><applet load="1cz7" size="350" color="white" frame="true" align="right" spinBox="true"
+
[[Image:1cz7.gif|left|200px]]
-
caption="1cz7, resolution 2.9&Aring;" />
+
 
-
'''THE CRYSTAL STRUCTURE OF A MINUS-END DIRECTED MICROTUBULE MOTOR PROTEIN NCD REVEALS VARIABLE DIMER CONFORMATIONS'''<br />
+
{{Structure
 +
|PDB= 1cz7 |SIZE=350|CAPTION= <scene name='initialview01'>1cz7</scene>, resolution 2.9&Aring;
 +
|SITE=
 +
|LIGAND= <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene> and <scene name='pdbligand=ADP:ADENOSINE-5'-DIPHOSPHATE'>ADP</scene>
 +
|ACTIVITY=
 +
|GENE=
 +
}}
 +
 
 +
'''THE CRYSTAL STRUCTURE OF A MINUS-END DIRECTED MICROTUBULE MOTOR PROTEIN NCD REVEALS VARIABLE DIMER CONFORMATIONS'''
 +
 
==Overview==
==Overview==
Line 7: Line 16:
==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 <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].
+
1CZ7 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Drosophila_melanogaster Drosophila melanogaster]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CZ7 OCA].
==Reference==
==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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=10574799 10574799]
+
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:[http://www.ncbi.nlm.nih.gov/pubmed/10574799 10574799]
[[Category: Drosophila melanogaster]]
[[Category: Drosophila melanogaster]]
[[Category: Single protein]]
[[Category: Single protein]]
Line 21: Line 30:
[[Category: MG]]
[[Category: MG]]
[[Category: kinesin superfamily]]
[[Category: kinesin superfamily]]
-
[[Category: microtubule motors]]
+
[[Category: microtubule motor]]
[[Category: ncd crystal structure]]
[[Category: ncd crystal structure]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:11:11 2008''
+
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:30:40 2008''

Revision as of 08:30, 20 March 2008


PDB ID 1cz7

Drag the structure with the mouse to rotate
, resolution 2.9Å
Ligands: and
Coordinates: save as pdb, mmCIF, xml



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. 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

Page seeded by OCA on Thu Mar 20 10:30:40 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools