4frz: Difference between revisions

Latest revision as of 15:33, 14 March 2024

Arabidopsis KCBP motor domain dimerized via regulatory domain

Structural highlights

4frz 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:	ADP, EDO, IMD, MG
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]

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:https://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:https://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:https://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:https://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:https://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:https://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

Proteopedia Page Contributors and Editors (what is this?)

OCA

[1] 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:https://dx.doi.org/10.1006/bbrc.1999.1896

[2] 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

[3] 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:https://dx.doi.org/10.1007/978-1-59745-490-2_2

[4] 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:https://dx.doi.org/10.1093/jxb/eru390

[5] 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:https://dx.doi.org/10.7554/eLife.09351

[6] 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

[7] 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:https://dx.doi.org/10.1073/pnas.94.1.322

[8] 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

[9] 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:https://dx.doi.org/10.1046/j.1365-313x.1997.12051139.x

[10] 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

[11] 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

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@@ Line 1: / Line 1: @@
-'''Unreleased structure'''
-The entry 4frz is ON HOLD
+==Arabidopsis KCBP motor domain dimerized via regulatory domain==
+<StructureSection load='4frz' size='340' side='right'caption='[[4frz]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
-Authors: Maia Vinogradova
+== Structural highlights ==
+<table><tr><td colspan='2'>[[4frz]] 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=4FRZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4FRZ FirstGlance]. <br>
-Description: Arabidopsis KCBP motor domain dimerized via regulatory domain
+</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='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=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=IMD:IMIDAZOLE'>IMD</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=4frz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4frz OCA], [https://pdbe.org/4frz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4frz RCSB], [https://www.ebi.ac.uk/pdbsum/4frz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4frz ProSAT]</span></td></tr>
+</table>
+== Function ==
+[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>
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Arabidopsis thaliana]]
+[[Category: Large Structures]]
+[[Category: Vinogradova M]]

4frz: Difference between revisions

Latest revision as of 15:33, 14 March 2024

Arabidopsis KCBP motor domain dimerized via regulatory domain

Structural highlights

Function

References

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