1b7t: Difference between revisions

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== Function ==
== Function ==
[[https://www.uniprot.org/uniprot/MYS_ARGIR MYS_ARGIR]] Muscle contraction.  Myosin is a protein that binds to F-actin and has ATPase activity that is activated by F-actin. [[https://www.uniprot.org/uniprot/MLE_ARGIR MLE_ARGIR]] In molluscan muscle, calcium regulation is associated with myosin rather than with actin. Muscle myosin contains two types of light chains: the catalytic light chain, essential for ATPase activity, and the regulatory light chain, a calcium-binding protein responsible for Ca(2+) dependent binding and Ca(2+) dependent Mg-ATPase activity. [[https://www.uniprot.org/uniprot/MLR_ARGIR MLR_ARGIR]] In molluscan muscle, calcium regulation is associated with myosin rather than with actin. Muscle myosin contains two types of light chains: the catalytic light chain, essential for ATPase activity, and the regulatory light chain, a calcium-binding protein responsible for Ca(2+) dependent binding and Ca(2+) dependent Mg-ATPase activity.  
[https://www.uniprot.org/uniprot/MYS_ARGIR MYS_ARGIR] Muscle contraction.  Myosin is a protein that binds to F-actin and has ATPase activity that is activated by F-actin.
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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[[Category: Myosin]]
[[Category: Myosin]]
[[Category: RCSB PDB Molecule of the Month]]
[[Category: RCSB PDB Molecule of the Month]]
[[Category: Cohen, C]]
[[Category: Cohen C]]
[[Category: Himmel, D]]
[[Category: Himmel D]]
[[Category: Houdusse, A]]
[[Category: Houdusse A]]
[[Category: Kalabokis, V]]
[[Category: Kalabokis V]]
[[Category: Szent-Gyorgyi, A G]]
[[Category: Szent-Gyorgyi AG]]
[[Category: Myosin motor]]

Revision as of 08:47, 31 May 2023

MYOSIN DIGESTED BY PAPAINMYOSIN DIGESTED BY PAPAIN

Structural highlights

1b7t is a 3 chain structure with sequence from Argopecten irradians. The June 2001 RCSB PDB Molecule of the Month feature on Myosin by David S. Goodsell is 10.2210/rcsb_pdb/mom_2001_6. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:, ,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

MYS_ARGIR Muscle contraction. Myosin is a protein that binds to F-actin and has ATPase activity that is activated by F-actin.

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

The crystal structure of a proteolytic subfragment from scallop striated muscle myosin, complexed with MgADP, has been solved at 2.5 A resolution and reveals an unusual conformation of the myosin head. The converter and the lever arm are in very different positions from those in either the pre-power stroke or near-rigor state structures; moreover, in contrast to these structures, the SH1 helix is seen to be unwound. Here we compare the overall organization of the myosin head in these three states and show how the conformation of three flexible "joints" produces rearrangements of the four major subdomains in the myosin head with different bound nucleotides. We believe that this novel structure represents one of the prehydrolysis ("ATP") states of the contractile cycle in which the myosin heads stay detached from actin.

Atomic structure of scallop myosin subfragment S1 complexed with MgADP: a novel conformation of the myosin head.,Houdusse A, Kalabokis VN, Himmel D, Szent-Gyorgyi AG, Cohen C Cell. 1999 May 14;97(4):459-70. PMID:10338210[1]

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

See Also

References

  1. ↑ Houdusse A, Kalabokis VN, Himmel D, Szent-Gyorgyi AG, Cohen C. Atomic structure of scallop myosin subfragment S1 complexed with MgADP: a novel conformation of the myosin head. Cell. 1999 May 14;97(4):459-70. PMID:10338210

1b7t, resolution 2.50Å

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OCA
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