Myosin

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{{STRUCTURE_3i5f| PDB=3i5f | SIZE=400| SCENE= |right|CAPTION=Squid myosin II: heavy chain (grey), regulatory light chain (green), catalytic light chain (pink) complex with ADP (stick model) and Mg+2 ion (green) [[3i5f]] }}
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<StructureSection load='3i5f' size='350' side='right' caption='Squid myosin II: heavy chain (grey), regulatory light chain (green), catalytic light chain (pink) complex with ADP and Mg+2 ion (green) [[3i5f]]' scene=''>
== Introduction ==
== Introduction ==
[[Myosin]] is one of three major classes of molecular motor proteins: myosin, dynein, and kinesin. As the most abundant of these proteins myosin plays a structural and enzymatic role in muscle contraction and intracellular motility. Myosin was first discovered in muscle in the 19th century. <ref name="Spudich">PMID: 8824453 </ref> Myosin is a superfamily of proteins which bind actin, hydrolyze ATP and transduce force. Thus most are located in muscle cells. Composed of head, neck and tail domains. Head domain binds the actin and moves along it. The neck is a linker and binds the light chains which have a regulatory function. The tail interacts with cargo molecules (CBD)m. There are 18 classes of myosin.<br />
[[Myosin]] is one of three major classes of molecular motor proteins: myosin, dynein, and kinesin. As the most abundant of these proteins myosin plays a structural and enzymatic role in muscle contraction and intracellular motility. Myosin was first discovered in muscle in the 19th century. <ref name="Spudich">PMID: 8824453 </ref> Myosin is a superfamily of proteins which bind actin, hydrolyze ATP and transduce force. Thus most are located in muscle cells. Composed of head, neck and tail domains. Head domain binds the actin and moves along it. The neck is a linker and binds the light chains which have a regulatory function. The tail interacts with cargo molecules (CBD)m. There are 18 classes of myosin.<br />
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'''Unconventional myosin''' are thought not to form filaments<ref>PMID:12471888</ref>.<br />
*'''Myosin II''' (MII) is best studied. It drives high-speed motility like muscle contraction<ref>PMID:15935670</ref>. MII contains 2 heavy chains (HC) which constitute the head or motor domain (MD) and the tail domain and 4 light chains (LC) which are referred to as the essential LC (ELC) and the regulatory LC (RLC). <br />
*'''Myosin II''' (MII) is best studied. It drives high-speed motility like muscle contraction<ref>PMID:15935670</ref>. MII contains 2 heavy chains (HC) which constitute the head or motor domain (MD) and the tail domain and 4 light chains (LC) which are referred to as the essential LC (ELC) and the regulatory LC (RLC). <br />
*'''Myosin III''' (MIII) contains a C-terminal kinase domain connected to the motor domain.
*'''Myosin III''' (MIII) contains a C-terminal kinase domain connected to the motor domain.
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*'''Myosin X''' (MX) is a downstream effector of PI(3)K during phagocytosis<ref>PMID:12055636</ref>.
*'''Myosin X''' (MX) is a downstream effector of PI(3)K during phagocytosis<ref>PMID:12055636</ref>.
*'''Myosin XI''' (MXI) links the nuclear membrane to the cytoskeleton<ref>PMID:23973298</ref>.
*'''Myosin XI''' (MXI) links the nuclear membrane to the cytoskeleton<ref>PMID:23973298</ref>.
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See also [[Myosin (hebrew)]].
==Crystallization and X-ray diffraction==
==Crystallization and X-ray diffraction==
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== 3D Structures of Myosin ==
== 3D Structures of Myosin ==
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[[Myosin 3D Structures]]
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Updated on {{REVISIONDAY2}}-{{MONTHNAME|{{REVISIONMONTH}}}}-{{REVISIONYEAR}}
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</StructureSection>
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{{#tree:id=OrganizedByTopic|openlevels=0|
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* Myosin I
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**[[1lkx]] – DdMI HC - ''Dictyostelium discoideum''<br />
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**[[4a7f]] - DdMI HC + rActin + rTropomyosin – rabbit – Cryo EM<br />
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**[[4a7h]], [[4a7l]] - DdMI HC (mutant) + rActin + rTropomyosin – Cryo EM<br />
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**[[2drk]], [[2drm]] – MI HC + 10-mer peptide – ''Acanthamoeba castellanii''<br />
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**[[2xmf]] – mMI SH3 domain - mouse<br />
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**[[4byf]] – hMIC + calmodulin – human<br />
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* Myosin II
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**[[1o1g]], [[1o1a]] , [[1o1b]], [[1o1c]], [[1o1d]], [[1o1e]], [[1o1f]], [[1o18]], [[1o19]], [[1mvw]], [[1m8q]] – cMII RLC+ELC+HC+actin – tomography - chicken<br />
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**[[3lla]] – cMII HC α-kinase domain+AMPPCP<br />
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**[[3lmh]] – cMII HC α-kinase domain+ADP<br />
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**[[3lmi]] – cMII HC α-kinase domain (mutant) +ATP<br />
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**[[2fxm]], [[2fxo]] – hMII HC S2 fragment <br />
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**[[2lnk]] – hMII HC + protein S100-A4 – NMR<br />
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**[[3zwh]] - hMII HC + protein S100-A4 (mutant)<br />
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**[[3i5f]] – LpMII RLC+HC+ADP+Mg – ''Loligo pealei''<br />
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**[[3i5g]], [[3i5h]] – LpMII RLC+HC+ELC<br />
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**[[3i5i]] – LpMII RLC+HC+ELC+SO4<br />
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**[[2jhr]] – DdMII HC+ADP-VO4+pentabromopseudilin<br />
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**[[2xo8]] - DdMII HC MD +pseudilin derivative<br />
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**[[2y0r]], [[2y8i]], [[2y9e]], [[3myk]] - DdMII HC MD (mutant)<br />
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**[[3bz7]], [[3bz9]], [[1yv3]], [[3bz8]] - DdMII HC+blebbistatin<br />
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**[[3mjx]] - DdMII HC+blebbistatin + ADP-VO4<br />
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**[[3mnq]] - DdMII HC MD + ADP-VO4 + reservatrol<br />
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**[[3bas]], [[3bat]], [[1fmv]] - DdMII HC<br />
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**[[1fmw]] – DdMII HC+ATP<br />
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**[[1jwy]], [[1jx2]] – DdMII HC+dynamin-1<br />
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**[[1d0x]], [[1d0y]], [[1d0z]], [[1d1a]], [[1d1b]], [[1d1c]] – DdMII HC (mutant)+BeF3 derivative<br />
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**[[1g8x]] – DdMII+actinin 3<br />
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**[[2jj9]], [[2x9h]] - DdMII HC+ADP-VO4<br />
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**[[3mkd]] - DdMII HC MD (mutant) + ADP-VO4 <br />
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**[[1lvk]], [[1mma]], [[1mmg]], [[1mmn]] – DdMII HC (mutant)+Mg+nucleotide<br />
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**[[1myh]], [[1myk]], [[1myl]], [[3myh]], [[3myl]] - DdMII HC (mutant)<br />
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**[[1mne]] - DdMII HC (mutant)+Mg+pyrophosphate<br />
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**[[1vom]] - DdMII HC (truncated)+Mg+ADP-VO4<br />
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**[[1mmd]], [[1w9i]], [[1w9k]] - DdMII HC (mutant)+Mg+ADP+BeF3<br />
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**[[1mnd]], [[1w9j]], [[1w9l]] - DdMII HC (mutant)+Mg+ADP+AlF4<br />
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**[[2aka]] - DdMII HC+dynamin-1<br />
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**[[2xel]], [[4ae3]] – DdMII HC + inhibitor<br />
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**[[1n2d]] – ScMII LC+IQ2 IQ3 motifs from Myo2p<br />
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**[[1m45]] - ScMII LC+IQ2 motif from Myo2p<br />
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**[[1m46]] - ScMII LC+IQ4 motif from Myo2p<br />
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**[[2bl0]] – MII RLC +RHC – ''Physarum polycephalum''
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* Myosin III
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**[[2btt]] – ScMIII SH3 domain – NMR<br />
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**[[1ruw]], [[1va7]] – yMIII SH3 domain
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*Myosin IV
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**[[3mmi]] – yMIV globular tail <br />
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**[[4ll6]] - yMIV globular tail (mutant)<br />
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**[[4ll8]] - yMIV globular tail (mutant) + SHE3P<br />
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* Myosin V (Unconventional myosin)
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**[[1w7i]] – cMV HC+LC+Mg+ADP<br />
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**[[1w7j]] - cMV HC+LC+BEFX+ADP<br />
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**[[1w8j]] – cMV HC<br />
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**[[1oe9]] – cMV HC+LC<br />
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**[[1br2]] – cMV HC+Mg+ADP+AlF4<br />
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**[[2fcd]] – ScMV LC N-terminal – ''Saccharomices cerevisiae'' – NMR<br />
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**[[2fce]] – ScMV LC C-terminal – NMR<br />
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**[[2f6h]] – ScMV CBD<br />
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**[[1yp5]], [[1zuy]] – yMV SH3 domain<br />
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**[[2ix7]] – mMV+apo-calmodulin <br />
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**[[3wb8]] – mMVA tail domain<br />
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**[[4j5l]], [[4j5m]] – hMVA tail domain<br />
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**[[4kp3]] – mMVA tail domain + RILP-like protein + melanophilin<br />
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**[[4lli]] – hMVA cargo binding domain<br />
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**[[4lx1]] – hMVA globular tail domain<br />
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**[[4lx2]] – hMVA globular tail domain + melanphilin<br />
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**[[4lnz]] – hMVB globular domain<br />
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**[[4lwz]], [[4lx0]] – hMVB globular tail + RAS-related protein<br />
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**[[4l8t]] – hMVC cargo binding domain<br />
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**[[4l79]] – raMIB + calmodulin - rat<br />
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* Myosin VI
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**[[2kia]] – mMVI CBD – mouse – NMR<br />
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**[[2ld3]] – mMVI lever arm extension - NMR<br />
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**[[3h8d]] - mMVI CBD+Dab2 peptide<br />
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**[[4e7z]] - pMVI<br />
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**[[4e7s]] - pMVI (mutant)<br />
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**[[3gn4]], [[2vb6]] - pMVI neck+calmodulin – pig<br />
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**[[2vas]], [[3l9i]] - pMVI neck (mutant)+calmodulin<br />
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**[[2v26]] - pMVI neck+Mg+ADP-VO4<br />
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**[[2bkh]], [[2bki]] – pMVI HC+calmodulin<br />
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**[[4dbp]], [[4dbq]] – pMVI HC (mutant) + calmodulin<br />
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**[[4dbr]] – pMVI HC (mutant) <br />
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**[[4anj]] - pMVI HC/GFP + calmodulin<br />
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**[[2x51]] - pMVI d insert1 + calmodulin
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*Myosin VII
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**[[2i0n]] - DdMVII SH3 domain - NMR<br />
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**[[3pvl]] - mMVII SH3 domain+hUsher syndrome type 1G protein<br />
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**[[4db1]] – hMVII HC
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*Myosin X
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**[[2lw9]] - hMX<br />
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**[[3au5]] - hMX myth4-ferm tandem<br />
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**[[3pzd]], [[3au4]] - hMX myth4-ferm tandem + netrin receptor DCC<br />
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**[[3tfm]] – raMX phin-ph2-phic tandem (mutant)
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*Myosin XI
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**[[3j04]] – cMXI HC + RLC – Cryo EM
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*Flight muscle myosin
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**[[1i84]], [[2w4a]], [[2w4g]], [[2w4h]] - cRLC+cELC+cHC – cryoEM<br />
 
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**[[2mys]] - cRLC+cELC+cHC - papain digested<br />
 
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**[[1lkm]] – cHC alpha-kinase domain+AMP<br />
 
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**[[2dfs]] – cHC+calmodulin<br />
 
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**[[1br4]] – cELC+cHC+Mg+ADP+BeF3<br />
 
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**[[1br1]] – cELC+Mg+ADP+AlF4<br />
 
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**[[2xrf]] – hLC <br />
 
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**[[3jtd]], [[2w4t]], [[2w4v]], [[2w4w]], [[1scm]] – AiRLC+AiELC+AiHC - ''Argopecten irradians''<br />
 
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**[[1b7t]] - AiRLC+AiELC+AiHC papain digested<br />
 
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**[[3jvt]] - sRLC+sELC+sHC+Ca – Scallop<br />
 
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**[[2ec6]], [[2os8]], [[2otg]], [[1s5g]], [[1sr6]], [[1qvi]], [[1kk7]], [[1dfk]], [[3pn7]], [[3ts5]], [[3tuy]] - sRLC+sELC+sHC<br />
 
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**[[1kqm]] - sRLC+sELC+sHC+AMPPNP<br />
 
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**[[1kwo]] - sRLC+sELC+sHC+ATPgS-PDM<br />
 
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**[[1l2o]] - sRLC+sELC+sHC+ADP-PDM<br />
 
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**[[1kk8]] - sRLC+sELC+sHC+ADP-BEFX<br />
 
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**[[1dfl]] - sRLC+sELC+sHC+ADP-VO4+Mg<br />
 
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**[[1wdc]] - sRLC+sELC+sHC - digested<br />
 
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**[[3dtp]] - RLC+HC+ELC – tarantula – Cryo EM
 
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}}
 
== References ==
== References ==
<references/>
<references/>
[[Category:Topic Page]]
[[Category:Topic Page]]

Current revision

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

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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