5jvr

From Proteopedia

(Difference between revisions)

Current revision

The neck-linker of Mus musculus KIF3A fused to the alpha 7 helix of Drosophila melanogaster Kinesin-1 fused to EB1

Structural highlights

5jvr is a 8 chain structure with sequence from Drosophila melanogaster, Homo sapiens and Mus musculus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 2.1Å
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

MARE1_HUMAN Binds to the plus end of microtubules and regulates the dynamics of the microtubule cytoskeleton. Promotes cytoplasmic microtubule nucleation and elongation. May be involved in spindle function by stabilizing microtubules and anchoring them at centrosomes. May play a role in cell migration.^[1] ^[2] ^[3] ^[4] KIF3A_MOUSE Microtubule-based anterograde translocator for membranous organelles. Plus end-directed microtubule sliding activity in vitro. Plays a role in primary cilia formation.^[5] KINH_DROME

Publication Abstract from PubMed

Kinesin-1, 2, 5, and 7 generate processive hand-over-hand 8-nm steps to transport intracellular cargoes toward the microtubule plus end. This processive motility requires gating mechanisms to coordinate the mechanochemical cycles of the two motor heads to sustain the processive run. A key structural element believed to regulate the degree of processivity is the neck-linker, a short peptide of 12-18 residues, which connects the motor domain to its coiled-coil stalk. While a shorter neck-linker has been correlated with longer run lengths, the structural data to support this hypothesis have been lacking. To test this hypothesis, seven kinesin structures were determined by X-ray crystallography. Each included the neck-linker motif, followed by helix alpha7 which constitutes the start of the coiled-coil stalk. In the majority of the structures, the neck-linker length differed from predictions because helix alpha7, which initiates the coiled-coil, started earlier in the sequence than predicted. A further examination of structures in the PDB reveals that there is a great disparity between the predicted and observed starting residues. This suggests that an accurate prediction of the start of a coiled-coil is currently difficult to achieve. These results are significant because they now exclude simple comparisons between members of the kinesin superfamily and add a further layer of complexity when interpreting the results of mutagenesis or protein fusion. They also re-emphasize the need to consider factors beyond the kinesin neck-linker motif when attempting to understand how inter-head communication is tuned to achieve the degree of processivity required for cellular function.

Family-specific kinesin structures reveal neck-linker length based on initiation of the coiled-coil.,Phillips RK, Peter LG, Gilbert SP, Rayment I J Biol Chem. 2016 Jul 26. pii: jbc.M116.737577. PMID:27462072^[6]

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

References

↑ Askham JM, Vaughan KT, Goodson HV, Morrison EE. Evidence that an interaction between EB1 and p150(Glued) is required for the formation and maintenance of a radial microtubule array anchored at the centrosome. Mol Biol Cell. 2002 Oct;13(10):3627-45. PMID:12388762 doi:10.1091/mbc.E02-01-0061
↑ van der Vaart B, Manatschal C, Grigoriev I, Olieric V, Gouveia SM, Bjelic S, Demmers J, Vorobjev I, Hoogenraad CC, Steinmetz MO, Akhmanova A. SLAIN2 links microtubule plus end-tracking proteins and controls microtubule growth in interphase. J Cell Biol. 2011 Jun 13;193(6):1083-99. Epub 2011 Jun 6. PMID:21646404 doi:10.1083/jcb.201012179
↑ Hayashi I, Wilde A, Mal TK, Ikura M. Structural basis for the activation of microtubule assembly by the EB1 and p150Glued complex. Mol Cell. 2005 Aug 19;19(4):449-60. PMID:16109370 doi:10.1016/j.molcel.2005.06.034
↑ Honnappa S, Gouveia SM, Weisbrich A, Damberger FF, Bhavesh NS, Jawhari H, Grigoriev I, van Rijssel FJ, Buey RM, Lawera A, Jelesarov I, Winkler FK, Wuthrich K, Akhmanova A, Steinmetz MO. An EB1-binding motif acts as a microtubule tip localization signal. Cell. 2009 Jul 23;138(2):366-76. PMID:19632184 doi:S0092-8674(09)00638-2
↑ Choi YH, Suzuki A, Hajarnis S, Ma Z, Chapin HC, Caplan MJ, Pontoglio M, Somlo S, Igarashi P. Polycystin-2 and phosphodiesterase 4C are components of a ciliary A-kinase anchoring protein complex that is disrupted in cystic kidney diseases. Proc Natl Acad Sci U S A. 2011 Jun 28;108(26):10679-84. doi:, 10.1073/pnas.1016214108. Epub 2011 Jun 13. PMID:21670265 doi:http://dx.doi.org/10.1073/pnas.1016214108
↑ Phillips RK, Peter LG, Gilbert SP, Rayment I. Family-specific kinesin structures reveal neck-linker length based on initiation of the coiled-coil. J Biol Chem. 2016 Jul 26. pii: jbc.M116.737577. PMID:27462072 doi:http://dx.doi.org/10.1074/jbc.M116.737577

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/5jvr"

@@ Line 1: / Line 1: @@
 ==The neck-linker of Mus musculus KIF3A fused to the alpha 7 helix of Drosophila melanogaster Kinesin-1 fused to EB1==
-<StructureSection load='5jvr' size='340' side='right' caption='[[5jvr]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
+<StructureSection load='5jvr' size='340' side='right'caption='[[5jvr]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[5jvr]] is a 8 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5JVR OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5JVR FirstGlance]. <br>
+<table><tr><td colspan='2'>[[5jvr]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Drosophila_melanogaster Drosophila melanogaster], [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5JVR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5JVR FirstGlance]. <br>
-</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5jv3|5jv3]], [[5jvm|5jvm]], [[5jvp|5jvp]], [[5jvs|5jvs]], [[5jvu|5jvu]], [[5jx1|5jx1]]</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]] 2.1&#8491;</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=5jvr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5jvr OCA], [http://pdbe.org/5jvr PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5jvr RCSB], [http://www.ebi.ac.uk/pdbsum/5jvr PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5jvr ProSAT]</span></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=5jvr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5jvr OCA], [https://pdbe.org/5jvr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5jvr RCSB], [https://www.ebi.ac.uk/pdbsum/5jvr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5jvr ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/KIF3A_MOUSE KIF3A_MOUSE]] Microtubule-based anterograde translocator for membranous organelles. Plus end-directed microtubule sliding activity in vitro. Plays a role in primary cilia formation.<ref>PMID:21670265</ref>
+[https://www.uniprot.org/uniprot/MARE1_HUMAN MARE1_HUMAN] Binds to the plus end of microtubules and regulates the dynamics of the microtubule cytoskeleton. Promotes cytoplasmic microtubule nucleation and elongation. May be involved in spindle function by stabilizing microtubules and anchoring them at centrosomes. May play a role in cell migration.<ref>PMID:12388762</ref> <ref>PMID:21646404</ref> <ref>PMID:16109370</ref> <ref>PMID:19632184</ref> [https://www.uniprot.org/uniprot/KIF3A_MOUSE KIF3A_MOUSE] Microtubule-based anterograde translocator for membranous organelles. Plus end-directed microtubule sliding activity in vitro. Plays a role in primary cilia formation.<ref>PMID:21670265</ref> [https://www.uniprot.org/uniprot/KINH_DROME KINH_DROME]
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
@@ Line 22: / Line 22: @@
 __TOC__
 </StructureSection>
-[[Category: Phillips, R K]]
+[[Category: Drosophila melanogaster]]
-[[Category: Rayment, I]]
+[[Category: Homo sapiens]]
-[[Category: Coiled-coil]]
+[[Category: Large Structures]]
-[[Category: Kinesin]]
+[[Category: Mus musculus]]
-[[Category: Motor protein]]
+[[Category: Phillips RK]]
+[[Category: Rayment I]]

5jvr

From Proteopedia

Current revision

The neck-linker of Mus musculus KIF3A fused to the alpha 7 helix of Drosophila melanogaster Kinesin-1 fused to EB1

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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