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PDBsum entry 4pfp

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protein ligands metals Protein-protein interface(s) links
Motor protein PDB id
4pfp

 

 

 

 

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JSmol PyMol  
Contents
Protein chains
760 a.a.
Ligands
ADP ×2
PGO
PO4 ×3
Metals
_MG ×2
Waters ×411
PDB id:
4pfp
Name: Motor protein
Title: Myosin vi motor domain in the pi release state (with pi) space group p21
Structure: Unconventional myosin-vi. Chain: a, c. Fragment: residues 2-789. Engineered: yes
Source: Sus scrofa. Pig. Organism_taxid: 9823. Gene: myo6. Expressed in: spodoptera frugiperda. Expression_system_taxid: 7108. Expression_system_cell_line: sf9.
Resolution:
2.32Å     R-factor:   0.191     R-free:   0.229
Authors: T.Isabet,H.Benisty,P.Llinas,H.L.Sweeney,A.Houdusse
Key ref: P.Llinas et al. (2015). How actin initiates the motor activity of Myosin. Dev Cell, 33, 401-412. PubMed id: 25936506 DOI: 10.1016/j.devcel.2015.03.025
Date:
30-Apr-14     Release date:   29-Apr-15    
PROCHECK
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 Headers
 References

Protein chains
Pfam   ArchSchema ?
F1RQI7  (F1RQI7_PIG) -  Unconventional myosin-VI from Sus scrofa
Seq:
Struc:
 
Seq:
Struc:
 
Seq:
Struc:
1266 a.a.
760 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 

 
DOI no: 10.1016/j.devcel.2015.03.025 Dev Cell 33:401-412 (2015)
PubMed id: 25936506  
 
 
How actin initiates the motor activity of Myosin.
P.Llinas, T.Isabet, L.Song, V.Ropars, B.Zong, H.Benisty, S.Sirigu, C.Morris, C.Kikuti, D.Safer, H.L.Sweeney, A.Houdusse.
 
  ABSTRACT  
 
Fundamental to cellular processes are directional movements driven by molecular motors. A common theme for these and other molecular machines driven by ATP is that controlled release of hydrolysis products is essential for using the chemical energy efficiently. Mechanochemical transduction by myosin motors on actin is coupled to unknown structural changes that result in the sequential release of inorganic phosphate (Pi) and MgADP. We present here a myosin structure possessing an actin-binding interface and a tunnel (back door) that creates an escape route for Pi with a minimal rotation of the myosin lever arm that drives movements. We propose that this state represents the beginning of the powerstroke on actin and that Pi translocation from the nucleotide pocket triggered by actin binding initiates myosin force generation. This elucidates how actin initiates force generation and movement and may represent a strategy common to many molecular machines.
 

 

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