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3h4s

From Proteopedia

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Current revision

Structure of the complex of a mitotic kinesin with its calcium binding regulator

Structural highlights

3h4s is a 2 chain structure with sequence from Arabidopsis thaliana. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 2.4Å
Ligands:	, ,
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

KN14E_ARATH Minus-end microtubule-dependent motor protein involved in the regulation of cell division and trichome morphogenesis through microtubules bundling. Possesses basal and microtubule-stimulated ATPase activities. Acts as a hub that brings together microtubules and actin filaments to modulate the cytoskeleton during trichome formation and morphogenesis (PubMed:26287478). Could be involved in the negative regulation of root growth (PubMed:25262228).^[1] ^[2] ^[3] ^[4] ^[5] ^[6] ^[7] ^[8] ^[9] ^[10] ^[11]

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 PubMed

Much of the transport, tension, and movement in mitosis depends on kinesins, the ATP-powered microtubule-based motors. We report the crystal structure of a kinesin complex, the mitotic kinesin KCBP bound to its principal regulator KIC. Shown to be a Ca(2+) sensor, KIC works as an allosteric trap. Extensive intermolecular interactions with KIC stabilize kinesin in its ADP-bound conformation. A critical component of the kinesin motile mechanism, called the neck mimic, switches its association from kinesin to KIC, stalling the motor. KIC denies access of the motor to its track by steric interference. Two major features of this regulation, allosteric trapping and steric blocking, are likely to be general for all kinesins.

Structure of the complex of a mitotic kinesin with its calcium binding regulator.,Vinogradova MV, Malanina GG, Reddy AS, Fletterick RJ Proc Natl Acad Sci U S A. 2009 May 19;106(20):8175-9. Epub 2009 May 5. PMID:19416847^[12]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Kao YL, Deavours BE, Phelps KK, Walker RA, Reddy AS. Bundling of microtubules by motor and tail domains of a kinesin-like calmodulin-binding protein from Arabidopsis: regulation by Ca(2+)/Calmodulin. Biochem Biophys Res Commun. 2000 Jan 7;267(1):201-7. doi: 10.1006/bbrc.1999.1896. PMID:10623599 doi:http://dx.doi.org/10.1006/bbrc.1999.1896
↑ Reddy VS, Day IS, Thomas T, Reddy AS. KIC, a novel Ca2+ binding protein with one EF-hand motif, interacts with a microtubule motor protein and regulates trichome morphogenesis. Plant Cell. 2004 Jan;16(1):185-200. Epub 2003 Dec 19. PMID:14688294 doi:10.1105/tpc.016600
↑ Reddy AS. Analysis of calcium/calmodulin regulation of a plant kinesin using co-sedimentation and ATPase assays. Methods Mol Biol. 2007;392:23-36. doi: 10.1007/978-1-59745-490-2_2. PMID:17951708 doi:http://dx.doi.org/10.1007/978-1-59745-490-2_2
↑ Humphrey TV, Haasen KE, Aldea-Brydges MG, Sun H, Zayed Y, Indriolo E, Goring DR. PERK-KIPK-KCBP signalling negatively regulates root growth in Arabidopsis thaliana. J Exp Bot. 2015 Jan;66(1):71-83. doi: 10.1093/jxb/eru390. Epub 2014 Sep 26. PMID:25262228 doi:http://dx.doi.org/10.1093/jxb/eru390
↑ Tian J, Han L, Feng Z, Wang G, Liu W, Ma Y, Yu Y, Kong Z. Orchestration of microtubules and the actin cytoskeleton in trichome cell shape determination by a plant-unique kinesin. Elife. 2015 Aug 19;4. doi: 10.7554/eLife.09351. PMID:26287478 doi:http://dx.doi.org/10.7554/eLife.09351
↑ Reddy AS, Safadi F, Narasimhulu SB, Golovkin M, Hu X. A novel plant calmodulin-binding protein with a kinesin heavy chain motor domain. J Biol Chem. 1996 Mar 22;271(12):7052-60. PMID:8636137
↑ Song H, Golovkin M, Reddy AS, Endow SA. In vitro motility of AtKCBP, a calmodulin-binding kinesin protein of Arabidopsis. Proc Natl Acad Sci U S A. 1997 Jan 7;94(1):322-7. doi: 10.1073/pnas.94.1.322. PMID:8990207 doi:http://dx.doi.org/10.1073/pnas.94.1.322
↑ Oppenheimer DG, Pollock MA, Vacik J, Szymanski DB, Ericson B, Feldmann K, Marks MD. Essential role of a kinesin-like protein in Arabidopsis trichome morphogenesis. Proc Natl Acad Sci U S A. 1997 Jun 10;94(12):6261-6. PMID:9177205
↑ Narasimhulu SB, Kao YL, Reddy AS. Interaction of Arabidopsis kinesin-like calmodulin-binding protein with tubulin subunits: modulation by Ca(2+)-calmodulin. Plant J. 1997 Nov;12(5):1139-49. doi: 10.1046/j.1365-313x.1997.12051139.x. PMID:9418053 doi:http://dx.doi.org/10.1046/j.1365-313x.1997.12051139.x
↑ Narasimhulu SB, Reddy AS. Characterization of microtubule binding domains in the Arabidopsis kinesin-like calmodulin binding protein. Plant Cell. 1998 Jun;10(6):957-65. PMID:9634584
↑ Deavours BE, Reddy AS, Walker RA. Ca2+/calmodulin regulation of the Arabidopsis kinesin-like calmodulin-binding protein. Cell Motil Cytoskeleton. 1998;40(4):408-16. PMID:9712269 doi:<408::AID-CM8>3.0.CO;2-6 10.1002/(SICI)1097-0169(1998)40:4<408::AID-CM8>3.0.CO;2-6
↑ Vinogradova MV, Malanina GG, Reddy AS, Fletterick RJ. Structure of the complex of a mitotic kinesin with its calcium binding regulator. Proc Natl Acad Sci U S A. 2009 May 19;106(20):8175-9. Epub 2009 May 5. PMID:19416847

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/3h4s"

Categories: Arabidopsis thaliana | Large Structures | Vinogradova MV

@@ Line 3: / Line 3: @@
 <StructureSection load='3h4s' size='340' side='right'caption='[[3h4s]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[3h4s]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Arath Arath]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3H4S OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3H4S FirstGlance]. <br>
+<table><tr><td colspan='2'>[[3h4s]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Arabidopsis_thaliana Arabidopsis thaliana]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3H4S OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3H4S FirstGlance]. <br>
-</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=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.4&#8491;</td></tr>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">At5g65930 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=3702 ARATH]), KIC ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=3702 ARATH])</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=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</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=3h4s FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3h4s OCA], [https://pdbe.org/3h4s PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3h4s RCSB], [https://www.ebi.ac.uk/pdbsum/3h4s PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3h4s ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[https://www.uniprot.org/uniprot/KCBP_ARATH KCBP_ARATH]] Minus-end microtubule-dependent motor protein involved in the regulation of cell division and trichome morphogenesis. Possesses basal and microtubule-stimulated ATPase activities.<ref>PMID:8636137</ref> <ref>PMID:9177205</ref> <ref>PMID:9712269</ref> <ref>PMID:9634584</ref> <ref>PMID:14688294</ref>  [[https://www.uniprot.org/uniprot/KIC_ARATH KIC_ARATH]] Calcium-binding regulatory protein that interacts with kinesin motor protein KCBP in a calcium-dependent manner. Inhibits KCBP microtubule binding activity and microtubule-stimulated ATPase activity. Involved in the regulation of trichome branching through its interaction with KCBP.<ref>PMID:14688294</ref>
+[https://www.uniprot.org/uniprot/KN14E_ARATH KN14E_ARATH] Minus-end microtubule-dependent motor protein involved in the regulation of cell division and trichome morphogenesis through microtubules bundling. Possesses basal and microtubule-stimulated ATPase activities. Acts as a hub that brings together microtubules and actin filaments to modulate the cytoskeleton during trichome formation and morphogenesis (PubMed:26287478). Could be involved in the negative regulation of root growth (PubMed:25262228).<ref>PMID:10623599</ref> <ref>PMID:14688294</ref> <ref>PMID:17951708</ref> <ref>PMID:25262228</ref> <ref>PMID:26287478</ref> <ref>PMID:8636137</ref> <ref>PMID:8990207</ref> <ref>PMID:9177205</ref> <ref>PMID:9418053</ref> <ref>PMID:9634584</ref> <ref>PMID:9712269</ref>
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 29: / Line 29: @@
 </div>
 <div class="pdbe-citations 3h4s" style="background-color:#fffaf0;"></div>
-==See Also==
-*[[Kinesin 3D Structures|Kinesin 3D Structures]]
 == References ==
 <references/>
 __TOC__
 </StructureSection>
-[[Category: Arath]]
+[[Category: Arabidopsis thaliana]]
 [[Category: Large Structures]]
-[[Category: Vinogradova, M V]]
+[[Category: Vinogradova MV]]
-[[Category: Atp-binding]]
-[[Category: Calcium]]
-[[Category: Calmodulin]]
-[[Category: Complex]]
-[[Category: Ef-hand]]
-[[Category: Kinesin]]
-[[Category: Microtubule]]
-[[Category: Motor protein]]
-[[Category: Motor protein-calcium binding protein complex]]
-[[Category: Nucleotide-binding]]
-[[Category: Regulation]]

3h4s

From Proteopedia

Current revision

Structure of the complex of a mitotic kinesin with its calcium binding regulator

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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