2ncd

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(New page: 200px<br /> <applet load="2ncd" size="450" color="white" frame="true" align="right" spinBox="true" caption="2ncd, resolution 2.5&Aring;" /> '''NCD (NON-CLARET DISJ...)
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<applet load="2ncd" size="450" color="white" frame="true" align="right" spinBox="true"
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caption="2ncd, resolution 2.5&Aring;" />
caption="2ncd, resolution 2.5&Aring;" />
'''NCD (NON-CLARET DISJUNCTIONAL) DIMER FROM D. MELANOGASTER'''<br />
'''NCD (NON-CLARET DISJUNCTIONAL) DIMER FROM D. MELANOGASTER'''<br />
==Overview==
==Overview==
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Motor proteins of the kinesin superfamily transport intracellular cargo, along microtubules. Although different kinesin proteins share 30-50%, amino-acid identity in their motor catalytic cores, some move to the plus, end of microtubules whereas others travel in the opposite direction., Crystal structures of the catalytic cores of conventional kinesin (a, plus-end-directed motor involved in organelle transport) and ncd (a, minus-end-directed motor involved in chromosome segregation) are nearly, identical; therefore, the structural basis for their opposite directions, of movement is unknown. Here we show that the ncd 'neck' made up of 13, class-specific residues next to the superfamily-conserved catalytic core, is essential for minus-end-directed motility, as mutagenesis of these neck, residues reverses the direction of ncd motion. By solving the 2.5 A, structure of a functional ncd dimer, we show that the ncd neck (a, coiled-coil) differs from the corresponding region in the kinesin neck (an, interrupted beta-strand), although both necks interact with similar, elements in the catalytic cores. The distinct neck architectures also, confer different symmetries to the ncd and kinesin dimers and position, these motors with appropriate directional bias on the microtubule.
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Motor proteins of the kinesin superfamily transport intracellular cargo along microtubules. Although different kinesin proteins share 30-50% amino-acid identity in their motor catalytic cores, some move to the plus end of microtubules whereas others travel in the opposite direction. Crystal structures of the catalytic cores of conventional kinesin (a plus-end-directed motor involved in organelle transport) and ncd (a minus-end-directed motor involved in chromosome segregation) are nearly identical; therefore, the structural basis for their opposite directions of movement is unknown. Here we show that the ncd 'neck' made up of 13 class-specific residues next to the superfamily-conserved catalytic core, is essential for minus-end-directed motility, as mutagenesis of these neck residues reverses the direction of ncd motion. By solving the 2.5 A structure of a functional ncd dimer, we show that the ncd neck (a coiled-coil) differs from the corresponding region in the kinesin neck (an interrupted beta-strand), although both necks interact with similar elements in the catalytic cores. The distinct neck architectures also confer different symmetries to the ncd and kinesin dimers and position these motors with appropriate directional bias on the microtubule.
==About this Structure==
==About this Structure==
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2NCD 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 SO4 and ADP as [http://en.wikipedia.org/wiki/ligands ligands]. The following page contains interesting information on the relation of 2NCD with [[http://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/pdb64_1.html Kinesin]]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2NCD OCA].
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2NCD 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=SO4:'>SO4</scene> and <scene name='pdbligand=ADP:'>ADP</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. The following page contains interesting information on the relation of 2NCD with [[http://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/pdb64_1.html Kinesin]]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2NCD OCA].
==Reference==
==Reference==
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[[Category: Kinesin]]
[[Category: Kinesin]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Case, R.B.]]
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[[Category: Case, R B.]]
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[[Category: Dai, S.C.]]
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[[Category: Dai, S C.]]
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[[Category: Fletterick, R.J.]]
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[[Category: Fletterick, R J.]]
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[[Category: Hart, C.L.]]
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[[Category: Hart, C L.]]
[[Category: Ruby, A.]]
[[Category: Ruby, A.]]
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[[Category: Sablin, E.P.]]
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[[Category: Sablin, E P.]]
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[[Category: Vale, R.D.]]
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[[Category: Vale, R D.]]
[[Category: ADP]]
[[Category: ADP]]
[[Category: SO4]]
[[Category: SO4]]
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[[Category: ncd]]
[[Category: ncd]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Sun Nov 18 09:09:09 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:08:12 2008''

Revision as of 16:08, 21 February 2008


2ncd, resolution 2.5Å

Drag the structure with the mouse to rotate

NCD (NON-CLARET DISJUNCTIONAL) DIMER FROM D. MELANOGASTER

Overview

Motor proteins of the kinesin superfamily transport intracellular cargo along microtubules. Although different kinesin proteins share 30-50% amino-acid identity in their motor catalytic cores, some move to the plus end of microtubules whereas others travel in the opposite direction. Crystal structures of the catalytic cores of conventional kinesin (a plus-end-directed motor involved in organelle transport) and ncd (a minus-end-directed motor involved in chromosome segregation) are nearly identical; therefore, the structural basis for their opposite directions of movement is unknown. Here we show that the ncd 'neck' made up of 13 class-specific residues next to the superfamily-conserved catalytic core, is essential for minus-end-directed motility, as mutagenesis of these neck residues reverses the direction of ncd motion. By solving the 2.5 A structure of a functional ncd dimer, we show that the ncd neck (a coiled-coil) differs from the corresponding region in the kinesin neck (an interrupted beta-strand), although both necks interact with similar elements in the catalytic cores. The distinct neck architectures also confer different symmetries to the ncd and kinesin dimers and position these motors with appropriate directional bias on the microtubule.

About this Structure

2NCD is a Single protein structure of sequence from Drosophila melanogaster with and as ligands. The following page contains interesting information on the relation of 2NCD with [Kinesin]. Full crystallographic information is available from OCA.

Reference

Direction determination in the minus-end-directed kinesin motor ncd., Sablin EP, Case RB, Dai SC, Hart CL, Ruby A, Vale RD, Fletterick RJ, Nature. 1998 Oct 22;395(6704):813-6. PMID:9796817

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