Myosin

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==Disease==
==Disease==
Mutations in MIIA cause early onset myopathy<ref>PMID:20418530</ref>. Mutations in MVIIA cause Usher syndrome<ref>PMID:7870171</ref>.
Mutations in MIIA cause early onset myopathy<ref>PMID:20418530</ref>. Mutations in MVIIA cause Usher syndrome<ref>PMID:7870171</ref>.
 +
 +
== 3D Structures of Myosin ==
 +
[[Myosin 3D Structures]]
 +
</StructureSection>
</StructureSection>
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* Myosin I
* Myosin I
 +
**[[4byf]] – hMIC + calmodulin – human<br />
 +
**[[2xmf]] – mMI SH3 domain - mouse<br />
 +
**[[5h53]] - rMI LC+HC + rActin – rabbit - Cryo EM<br />
**[[1lkx]], [[5ejy]] – DdMI HC - ''Dictyostelium discoideum''<br />
**[[1lkx]], [[5ejy]] – DdMI HC - ''Dictyostelium discoideum''<br />
**[[5ejs]] – DdMI HC (mutant)<br />
**[[5ejs]] – DdMI HC (mutant)<br />
-
**[[4a7f]] - DdMI HC + rActin + rTropomyosin – rabbit – Cryo EM<br />
+
**[[4a7f]] - DdMI HC + rActin + rTropomyosin – Cryo EM<br />
**[[4a7h]], [[4a7l]] - DdMI HC (mutant) + rActin + rTropomyosin – Cryo EM<br />
**[[4a7h]], [[4a7l]] - DdMI HC (mutant) + rActin + rTropomyosin – Cryo EM<br />
**[[5ibw]] – DdMIC HC + Ca-binding protein <br />
**[[5ibw]] – DdMIC HC + Ca-binding protein <br />
**[[2drk]], [[2drm]] – MI HC + 10-mer peptide – ''Acanthamoeba castellanii''<br />
**[[2drk]], [[2drm]] – MI HC + 10-mer peptide – ''Acanthamoeba castellanii''<br />
-
**[[2xmf]] – mMI SH3 domain - mouse<br />
+
**[[6i7e]], [[6i7d]] – MI – ''Plasmodium falciparum''<br />
-
**[[4byf]] – hMIC + calmodulin – human<br />
+
-
**[[5h53]] - rMI LC+HC + rActin – Cryo EM<br />
+
*Unconventional myosin I
*Unconventional myosin I
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**[[4l79]] – raMIB + calmodulin <br />
**[[4l79]] – raMIB + calmodulin <br />
**[[6c1d]] – raMIB + calmodulin + actin + phalloidin – Cryo EM<br />
**[[6c1d]] – raMIB + calmodulin + actin + phalloidin – Cryo EM<br />
-
**[[5xgg]], [[5xg9]] – MIB C-terminal SH3 – ''Entamoeba histolytica''<br />
 
**[[4r8g]] – mMIC C-terminal + calmodulin<br />
**[[4r8g]] – mMIC C-terminal + calmodulin<br />
 +
**[[5xgg]], [[5xg9]] – EhMIB C-terminal SH3 – ''Entamoeba histolytica''<br />
 +
**[[6a9c]] – EhMIB C-terminal SH3 + FP10 peptide<br />
* Myosin II
* Myosin II
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**[[2aka]] - DdMII HC+dynamin-1<br />
**[[2aka]] - DdMII HC+dynamin-1<br />
**[[2xel]], [[4ae3]] – DdMII HC + inhibitor<br />
**[[2xel]], [[4ae3]] – DdMII HC + inhibitor<br />
-
**[[1n2d]] – ScMII LC+IQ2 IQ3 motifs from Myo2p<br />
+
**[[6ixo]] – yMII GTD - yeast<br />
-
**[[1m45]] - ScMII LC+IQ2 motif from Myo2p<br />
+
**[[1n2d]] – yMII LC+IQ2 IQ3 motifs from Myo2p<br />
-
**[[1m46]] - ScMII LC+IQ4 motif from Myo2p<br />
+
**[[1m45]] - yMII LC+IQ2 motif from Myo2p<br />
 +
**[[1m46]] - yMII LC+IQ4 motif from Myo2p<br />
 +
**[[6ixr]], [[6ixq]], [[6ixp]] – yMII GTD (mutant) + peptide<br />
**[[2bl0]] – MII RLC +RHC – ''Physarum polycephalum''<br />
**[[2bl0]] – MII RLC +RHC – ''Physarum polycephalum''<br />
**[[5w1a]] - MII HC MD + LC – ''Drosophila melanogaster''<br />
**[[5w1a]] - MII HC MD + LC – ''Drosophila melanogaster''<br />
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*Myosin IV
*Myosin IV
-
**[[3mmi]] – yMIV globular tail <br />
+
**[[3mmi]] – yMIV GTD <br />
-
**[[4ll6]] - yMIV globular tail (mutant)<br />
+
**[[4ll6]] - yMIV GTD (mutant)<br />
-
**[[4ll8]] - yMIV globular tail (mutant) + SHE3P<br />
+
**[[4ll8]] - yMIV GTD (mutant) + SHE3P<br />
 +
**[[6qdj]] – MIV – ''Caenorhabditis elegans'' <br />
 +
 
 +
*Myosin V
 +
 
 +
**[[6eyw]] - yMV CBD<br />
* Myosin V (Unconventional myosin)
* Myosin V (Unconventional myosin)
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**[[4zlk]] - mMVA + calmodulin<br />
**[[4zlk]] - mMVA + calmodulin<br />
**[[2ix7]] – mMVA IQ motif +apo-calmodulin <br />
**[[2ix7]] – mMVA IQ motif +apo-calmodulin <br />
-
**[[3wb8]] – mMVA tail domain<br />
+
**[[3wb8]] – mMVA GTD<br />
-
**[[4j5l]], [[4j5m]] – hMVA tail domain<br />
+
**[[4j5l]], [[4j5m]] – hMVA GTD<br />
-
**[[4kp3]] – mMVA tail domain + RILP-like protein + melanophilin<br />
+
**[[4kp3]] – mMVA GTD + RILP-like protein + melanophilin<br />
-
**[[4lli]] – hMVA cargo binding domain<br />
+
**[[4lli]] – hMVA CBD<br />
-
**[[4lx1]] – hMVA globular tail domain<br />
+
**[[4lx1]] – hMVA GTD<br />
-
**[[4lx2]] – hMVA globular tail domain + melanphilin<br />
+
**[[4lx2]] – hMVA GTD + melanphilin<br />
-
**[[5jcz]] – hMVA globular tail domain + RAB-11<br />
+
**[[5jcz]] – hMVA GTD + RAB-11<br />
-
**[[5jcy]] – hMVA globular tail domain + SPIR-2<br />
+
**[[5jcy]] – hMVA GTD + SPIR-2<br />
-
**[[4lnz]] – hMVB globular domain<br />
+
**[[4lnz]] – hMVB GTD<br />
-
**[[4lwz]], [[4lx0]] – hMVB globular tail + RAS-related protein<br />
+
**[[4lwz]], [[4lx0]] – hMVB GTD + RAS-related protein<br />
**[[5hmp]], [[4zg4]] – hMVC <br />
**[[5hmp]], [[4zg4]] – hMVC <br />
-
**[[4l8t]] – hMVC cargo binding domain<br />
+
**[[4l8t]] – hMVC CBD<br />
* Myosin VI
* Myosin VI
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**[[6bnw]], [[6bnq]], [[6bnp]] – pMVI + actin – Cryo EM<br />
**[[6bnw]], [[6bnq]], [[6bnp]] – pMVI + actin – Cryo EM<br />
**[[6bnv]] – pMVI + actin + calmodulin – Cryo EM<br />
**[[6bnv]] – pMVI + actin + calmodulin – Cryo EM<br />
 +
**[[6bnv]] – MVI residus 1-69 – ''Meriones unguiculatus''<br />
*Unconventional myosin VI
*Unconventional myosin VI
 +
**[[6j56]] – hMVI CBD + TOM1 peptide <br />
**[[5v6h]] – mMVI + GIPC2 <br />
**[[5v6h]] – mMVI + GIPC2 <br />
**[[5v6e]] – mMVI + GIPC1 <br />
**[[5v6e]] – mMVI + GIPC1 <br />
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**[[5c5s]] – hMIXB RHOGAP domain <br />
**[[5c5s]] – hMIXB RHOGAP domain <br />
-
**[[5hpy]] – hMIXB motor domain + RHOA <br />
+
**[[5hpy]] – hMIXB MD + RHOA <br />
*Myosin X
*Myosin X
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*Unconventional myosin X
*Unconventional myosin X
-
**[[5i0h]] – hMX motor domain <br />
+
**[[5i0h]] – hMX MD <br />
-
**[[5kg8]] – hMX motor domain + actin <br />
+
**[[5kg8]] – hMX MD + actin <br />
-
**[[5i0i]] – hMX motor domain + calmodulin <br />
+
**[[5i0i]] – hMX MD + calmodulin <br />
**[[5hmo]] – MX SAH + coiled-coil domain - bovine <br />
**[[5hmo]] – MX SAH + coiled-coil domain - bovine <br />
*Myosin XI
*Myosin XI
-
**[[5t45]] – cMXI motor domain <br />
+
**[[5t45]] – cMXI MD <br />
-
**[[5m05]] – cMXI motor domain + inhibitor <br />
+
**[[5m05]] – cMXI MD + inhibitor <br />
-
**[[3j04]] – cMXI HC + RLC – Cryo EM
+
**[[3j04]] – cMXI HC + RLC – Cryo EM<br />
 +
**[[6bih]] – cMXI HC + actin – Cryo EM<br />
 +
 
 +
*Unconventional myosin XIV
 +
 
 +
**[[6due]] – MXIV – ''Toxoplasma gondii'' <br />
*Flight muscle myosin
*Flight muscle myosin

Revision as of 10:07, 5 November 2019

Squid myosin II: heavy chain (grey), regulatory light chain (green), catalytic light chain (pink) complex with ADP and Mg+2 ion (green) 3i5f

Drag the structure with the mouse to rotate

3D Structures of Myosin

Updated on 05-November-2019

References

  1. ↑ Spudich JA, Finer J, Simmons B, Ruppel K, Patterson B, Uyeda T. Myosin structure and function. Cold Spring Harb Symp Quant Biol. 1995;60:783-91. PMID:8824453
  2. ↑ Kalhammer G, Bahler M. Unconventional myosins. Essays Biochem. 2000;35:33-42. PMID:12471888
  3. ↑ Matsumura F. Regulation of myosin II during cytokinesis in higher eukaryotes. Trends Cell Biol. 2005 Jul;15(7):371-7. PMID:15935670 doi:http://dx.doi.org/10.1016/j.tcb.2005.05.004
  4. ↑ Mehta AD, Rock RS, Rief M, Spudich JA, Mooseker MS, Cheney RE. Myosin-V is a processive actin-based motor. Nature. 1999 Aug 5;400(6744):590-3. PMID:10448864 doi:http://dx.doi.org/10.1038/23072
  5. ↑ Buss F, Spudich G, Kendrick-Jones J. Myosin VI: cellular functions and motor properties. Annu Rev Cell Dev Biol. 2004;20:649-76. PMID:15473855 doi:http://dx.doi.org/10.1146/annurev.cellbio.20.012103.094243
  6. ↑ Hasson T, Skowron JF, Gilbert DJ, Avraham KB, Perry WL, Bement WM, Anderson BL, Sherr EH, Chen ZY, Greene LA, Ward DC, Corey DP, Mooseker MS, Copeland NG, Jenkins NA. Mapping of unconventional myosins in mouse and human. Genomics. 1996 Sep 15;36(3):431-9. PMID:8884266 doi:http://dx.doi.org/10.1006/geno.1996.0488
  7. ↑ Cox D, Berg JS, Cammer M, Chinegwundoh JO, Dale BM, Cheney RE, Greenberg S. Myosin X is a downstream effector of PI(3)K during phagocytosis. Nat Cell Biol. 2002 Jul;4(7):469-77. PMID:12055636 doi:http://dx.doi.org/10.1038/ncb805
  8. ↑ Tamura K, Iwabuchi K, Fukao Y, Kondo M, Okamoto K, Ueda H, Nishimura M, Hara-Nishimura I. Myosin XI-i links the nuclear membrane to the cytoskeleton to control nuclear movement and shape in Arabidopsis. Curr Biol. 2013 Sep 23;23(18):1776-81. doi: 10.1016/j.cub.2013.07.035. Epub 2013 , Aug 22. PMID:23973298 doi:http://dx.doi.org/10.1016/j.cub.2013.07.035
  9. ↑ 9.0 9.1 9.2 9.3 9.4 9.5 Rayment I, Rypniewski WR, Schmidt-Base K, Smith R, Tomchick DR, Benning MM, Winkelmann DA, Wesenberg G, Holden HM. Three-dimensional structure of myosin subfragment-1: a molecular motor. Science. 1993 Jul 2;261(5117):50-8. PMID:8316857
  10. ↑ 10.0 10.1 10.2 Nelson, D. and Cox, M.(2005). Lehninger Principles of Biochemistry. 4th ed. p.1119.
  11. ↑ Tajsharghi H, Hilton-Jones D, Raheem O, Saukkonen AM, Oldfors A, Udd B. Human disease caused by loss of fast IIa myosin heavy chain due to recessive MYH2 mutations. Brain. 2010 May;133(Pt 5):1451-9. doi: 10.1093/brain/awq083. PMID:20418530 doi:http://dx.doi.org/10.1093/brain/awq083
  12. ↑ Weil D, Blanchard S, Kaplan J, Guilford P, Gibson F, Walsh J, Mburu P, Varela A, Levilliers J, Weston MD, et al.. Defective myosin VIIA gene responsible for Usher syndrome type 1B. Nature. 1995 Mar 2;374(6517):60-1. PMID:7870171 doi:http://dx.doi.org/10.1038/374060a0
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