2ncd: Difference between revisions
No edit summary |
No edit summary |
||
| (6 intermediate revisions by the same user not shown) | |||
| Line 1: | Line 1: | ||
==NCD (NON-CLARET DISJUNCTIONAL) DIMER FROM D. MELANOGASTER== | |||
<StructureSection load='2ncd' size='340' side='right'caption='[[2ncd]], [[Resolution|resolution]] 2.50Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[2ncd]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Drosophila_melanogaster Drosophila melanogaster]. The April 2005 RCSB PDB [https://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/index.html Molecule of the Month] feature on ''Kinesin'' by David S. Goodsell is [https://dx.doi.org/10.2210/rcsb_pdb/mom_2005_4 10.2210/rcsb_pdb/mom_2005_4]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2NCD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2NCD FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.5Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2ncd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ncd OCA], [https://pdbe.org/2ncd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2ncd RCSB], [https://www.ebi.ac.uk/pdbsum/2ncd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2ncd ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/NCD_DROME NCD_DROME] NCD is required for normal chromosomal segregation in meiosis, in females, and in early mitotic divisions of the embryo. The NCD motor activity is directed toward the microtubule's minus end.<ref>PMID:2146510</ref> | |||
== Evolutionary Conservation == | |||
[[Image:Consurf_key_small.gif|200px|right]] | |||
Check<jmol> | |||
<jmolCheckbox> | |||
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/nc/2ncd_consurf.spt"</scriptWhenChecked> | |||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | |||
<text>to colour the structure by Evolutionary Conservation</text> | |||
</jmolCheckbox> | |||
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2ncd ConSurf]. | |||
<div style="clear:both"></div> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
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. | |||
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<ref>PMID:9796817</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 2ncd" style="background-color:#fffaf0;"></div> | |||
==See Also== | ==See Also== | ||
*[[Kinesin|Kinesin]] | *[[Kinesin 3D Structures|Kinesin 3D Structures]] | ||
== References == | |||
== | <references/> | ||
< | __TOC__ | ||
</StructureSection> | |||
[[Category: Drosophila melanogaster]] | [[Category: Drosophila melanogaster]] | ||
[[Category: Kinesin]] | [[Category: Kinesin]] | ||
[[Category: Large Structures]] | |||
[[Category: RCSB PDB Molecule of the Month]] | [[Category: RCSB PDB Molecule of the Month]] | ||
[[Category: Case | [[Category: Case RB]] | ||
[[Category: Dai | [[Category: Dai SC]] | ||
[[Category: Fletterick | [[Category: Fletterick RJ]] | ||
[[Category: Hart | [[Category: Hart CL]] | ||
[[Category: Ruby | [[Category: Ruby A]] | ||
[[Category: Sablin | [[Category: Sablin EP]] | ||
[[Category: Vale | [[Category: Vale RD]] | ||
Latest revision as of 03:08, 28 December 2023
NCD (NON-CLARET DISJUNCTIONAL) DIMER FROM D. MELANOGASTERNCD (NON-CLARET DISJUNCTIONAL) DIMER FROM D. MELANOGASTER
Structural highlights
FunctionNCD_DROME NCD is required for normal chromosomal segregation in meiosis, in females, and in early mitotic divisions of the embryo. The NCD motor activity is directed toward the microtubule's minus end.[1] Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedMotor 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. 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[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
|
| ||||||||||||||||||