PDBsum entry 4anj

Motor protein/metal-bindng protein

PDB id: 4anj

Contents

Protein chains

996 a.a.

128 a.a.

Ligands

ADP

ALF

Metals

_CA ×3

_MG

Waters ×91

PDB id:

4anj

Name:

Motor protein/metal-bindng protein

Title:

Myosin vi (mdinsert2-gfp fusion) pre-powerstroke state (mg.Adp.Alf4)

Structure:

Unconventional myosin-vi, green fluorescent protein. Chain: a. Fragment: myosin-6 residues 1-817, gfp residues 2-238. Synonym: unconventional myosin-6. Engineered: yes. Other_details: chimeric protein, myosin-6 residues 1-816 (author numbering) and complete gfp (after initiation methionine removal). Calmodulin. Chain: b.

Source:

Sus scrofa, aequorea victoria. Pig, jellyfish. Organism_taxid: 9823, 6100. Expressed in: spodoptera frugiperda. Expression_system_taxid: 7108. Expression_system_cell_line: sf9. Drosophila melanogaster. Fruit fly. Organism_taxid: 7227.

Resolution:

2.60Å R-factor: 0.241 R-free: 0.288

Authors:

J.Menetrey,T.Isabet,V.Ropars,M.Mukherjea,O.Pylypenko,X.Liu,J.Perez, P.Vachette,H.L.Sweeney,A.M.Houdusse

Key ref:

J.Ménétrey et al. (2012). Processive steps in the reverse direction require uncoupling of the lead head lever arm of myosin VI. Mol Cell, 48, 75-86. PubMed id: 22940248

Date:

19-Mar-12 Release date: 17-Oct-12

Protein chain

P42212  (GFP_AEQVI) -  Green fluorescent protein from Aequorea victoria

Seq: 238 a.a.

Struc: 996 a.a.*

Protein chain

Q29122  (MYO6_PIG) -  Unconventional myosin-VI from Sus scrofa

Seq: 1254 a.a.

Struc: 996 a.a.*

Protein chain

P62152  (CALM_DROME) -  Calmodulin from Drosophila melanogaster

Seq: 149 a.a.

Struc: 128 a.a.

* PDB and UniProt seqs differ at 220 residue positions (black crosses)

Mol Cell 48:75-86 (2012)

PubMed id: 22940248

Processive steps in the reverse direction require uncoupling of the lead head lever arm of myosin VI.

J.Ménétrey, T.Isabet, V.Ropars, M.Mukherjea, O.Pylypenko, X.Liu, J.Perez, P.Vachette, H.L.Sweeney, A.M.Houdusse.

ABSTRACT

Myosin VI is the only known reverse-direction myosin motor. It has an unprecedented means of amplifying movements within the motor involving rearrangements of the converter subdomain at the C terminus of the motor and an unusual lever arm projecting from the converter. While the average step size of a myosin VI dimer is 30-36 nm, the step size is highly variable, presenting a challenge to the lever arm mechanism by which all myosins are thought to move. Herein, we present structures of myosin VI that reveal regions of compliance that allow an uncoupling of the lead head when movement is modeled on actin. The location of the compliance restricts the possible actin binding sites and predicts the observed stepping behavior. The model reveals that myosin VI, unlike plus-end directed myosins, does not use a pure lever arm mechanism, but instead steps with a mechanism analogous to the kinesin neck-linker uncoupling model.