3h4s: Difference between revisions

Revision as of 17:02, 24 December 2014

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.
Ligands:	ADP, CA, MG
Gene:	At5g65930 (Arabidopsis thaliana), KIC (Arabidopsis thaliana)
Resources:	FirstGlance, OCA, RCSB, PDBsum

Function

[Q9FHN8_ARATH] Minus-end microtubule-dependent motor protein involved in the regulation of cell division and trichome morphogenesis. Possesses basal and microtubule-stimulated ATPase activities.^[1] ^[2] ^[3] ^[4] ^[5] [Q9ZPX9_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.^[6]

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^[7]

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

References

↑ 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
↑ 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
↑ 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
↑ 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
↑ 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 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
↑ 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

Proteopedia Page Contributors and Editors (what is this?)

OCA

[1] 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

[2] 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

[3] 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

[4] 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

[5] 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

[6] 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

[7] 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]

[2]

[3]

[4]

[5]

[6]

[7]

@@ Line 3: / Line 3: @@
 == Structural highlights ==
 <table><tr><td colspan='2'>[[3h4s]] is a 2 chain structure with sequence from [http://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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3H4S FirstGlance]. <br>
-</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><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><br>
+</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><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><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">At5g65930 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=3702 Arabidopsis thaliana]), KIC ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=3702 Arabidopsis thaliana])</td></tr>
+<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">At5g65930 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=3702 Arabidopsis thaliana]), KIC ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=3702 Arabidopsis thaliana])</td></tr>
-<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3h4s FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3h4s OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3h4s RCSB], [http://www.ebi.ac.uk/pdbsum/3h4s PDBsum]</span></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3h4s FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3h4s OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3h4s RCSB], [http://www.ebi.ac.uk/pdbsum/3h4s PDBsum]</span></td></tr>
-<table>
+</table>
+== Function ==
+[[http://www.uniprot.org/uniprot/Q9FHN8_ARATH Q9FHN8_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>  [[http://www.uniprot.org/uniprot/Q9ZPX9_ARATH Q9ZPX9_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>
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 33: / Line 35: @@
 </StructureSection>
 [[Category: Arabidopsis thaliana]]
-[[Category: Vinogradova, M V.]]
+[[Category: Vinogradova, M V]]
 [[Category: Atp-binding]]
 [[Category: Calmodulin]]

3h4s: Difference between revisions

Revision as of 17:02, 24 December 2014

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

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Navigation menu

Page actions

Page actions

Personal tools

Navigation

Search

Tools