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5et1

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Current revision

Crystal structure of Myo3b-ARB1 in complex with Espin1-AR

Structural highlights

5et1 is a 4 chain structure with sequence from Mus musculus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 1.65Å
Ligands:
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

ESPN_MOUSE Multifunctional actin-bundling protein. Plays a major role in regulating the organization, dimensions, dynamics and signaling capacities of the actin filament-rich, microvillus-type specializations that mediate sensory transduction in variouS mechanosensory and chemosensory cells.^[1] ^[2]

Publication Abstract from PubMed

Class III myosins (Myo3) and actin-bundling protein Espin play critical roles in regulating the development and maintenance of stereocilia in vertebrate hair cells, and their defects cause hereditary hearing impairments. Myo3 interacts with Espin1 through its tail homology I motif (THDI), however it is not clear how Myo3 specifically acts through Espin1 to regulate the actin bundle assembly and stabilization. Here we discover that Myo3 THDI contains a pair of repeat sequences capable of independently and strongly binding to the ankyrin repeats of Espin1, revealing an unexpected Myo3-mediated cross-linking mechanism of Espin1. The structures of Myo3 in complex with Espin1 not only elucidate the mechanism of the binding, but also reveal a Myo3-induced release of Espin1 auto-inhibition mechanism. We also provide evidence that Myo3-mediated cross-linking can further promote actin fiber bundling activity of Espin1.

Myosin III-mediated cross-linking and stimulation of actin bundling activity of Espin.,Liu H, Li J, Raval MH, Yao N, Deng X, Lu Q, Nie S, Feng W, Wan J, Yengo CM, Liu W, Zhang M Elife. 2016 Jan 19;5. pii: e12856. doi: 10.7554/eLife.12856. PMID:26785147^[3]

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

References

↑ Loomis PA, Zheng L, Sekerkova G, Changyaleket B, Mugnaini E, Bartles JR. Espin cross-links cause the elongation of microvillus-type parallel actin bundles in vivo. J Cell Biol. 2003 Dec 8;163(5):1045-55. Epub 2003 Dec 1. PMID:14657236 doi:http://dx.doi.org/10.1083/jcb.200309093
↑ Sekerkova G, Zheng L, Loomis PA, Changyaleket B, Whitlon DS, Mugnaini E, Bartles JR. Espins are multifunctional actin cytoskeletal regulatory proteins in the microvilli of chemosensory and mechanosensory cells. J Neurosci. 2004 Jun 9;24(23):5445-56. PMID:15190118 doi:http://dx.doi.org/10.1523/JNEUROSCI.1279-04.2004
↑ Liu H, Li J, Raval MH, Yao N, Deng X, Lu Q, Nie S, Feng W, Wan J, Yengo CM, Liu W, Zhang M. Myosin III-mediated cross-linking and stimulation of actin bundling activity of Espin. Elife. 2016 Jan 19;5. pii: e12856. doi: 10.7554/eLife.12856. PMID:26785147 doi:http://dx.doi.org/10.7554/eLife.12856

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/5et1"

@@ Line 1: / Line 1: @@
 ==Crystal structure of Myo3b-ARB1 in complex with Espin1-AR==
-<StructureSection load='5et1' size='340' side='right' caption='[[5et1]], [[Resolution|resolution]] 1.65&Aring;' scene=''>
+<StructureSection load='5et1' size='340' side='right'caption='[[5et1]], [[Resolution|resolution]] 1.65&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[5et1]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5ET1 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5ET1 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[5et1]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5ET1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5ET1 FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</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]] 1.65&#8491;</td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5et0|5et0]]</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></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=5et1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5et1 OCA], [http://pdbe.org/5et1 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5et1 RCSB], [http://www.ebi.ac.uk/pdbsum/5et1 PDBsum]</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=5et1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5et1 OCA], [https://pdbe.org/5et1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5et1 RCSB], [https://www.ebi.ac.uk/pdbsum/5et1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5et1 ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/ESPN_MOUSE ESPN_MOUSE]] Multifunctional actin-bundling protein. Plays a major role in regulating the organization, dimensions, dynamics and signaling capacities of the actin filament-rich, microvillus-type specializations that mediate sensory transduction in variouS mechanosensory and chemosensory cells.<ref>PMID:14657236</ref> <ref>PMID:15190118</ref>  [[http://www.uniprot.org/uniprot/MYO3B_MOUSE MYO3B_MOUSE]] Probable actin-based motor with a protein kinase activity.
+[https://www.uniprot.org/uniprot/ESPN_MOUSE ESPN_MOUSE] Multifunctional actin-bundling protein. Plays a major role in regulating the organization, dimensions, dynamics and signaling capacities of the actin filament-rich, microvillus-type specializations that mediate sensory transduction in variouS mechanosensory and chemosensory cells.<ref>PMID:14657236</ref> <ref>PMID:15190118</ref>
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
@@ Line 22: / Line 23: @@
 __TOC__
 </StructureSection>
-[[Category: Li, J]]
+[[Category: Large Structures]]
-[[Category: Liu, H]]
+[[Category: Mus musculus]]
-[[Category: Zhang, M]]
+[[Category: Li J]]
-[[Category: Liu, W]]
+[[Category: Liu H]]
-[[Category: Complex]]
+[[Category: Zhang M]]
-[[Category: Protein binding]]
+[[Category: Liu W]]
-[[Category: Protein binding-motor protein complex]]
-[[Category: Unconventional myosin]]

5et1

From Proteopedia

Current revision

Crystal structure of Myo3b-ARB1 in complex with Espin1-AR

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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