PDBsum entry 4byf

Hydrolase

PDB id: 4byf

Contents

Protein chains

698 a.a.

148 a.a.

Ligands

AOV ×2

Metals

_MG ×3

Waters ×194

PDB id:

4byf

Name:

Hydrolase

Title:

Crystal structure of human myosin 1c in complex with calmodulin in the pre-power stroke state

Structure:

Unconventional myosin-ic. Chain: a, c. Fragment: motor domain, residues 36-760. Synonym: myosin i beta, mmi-beta, mmib. Engineered: yes. Calmodulin. Chain: b, d. Synonym: cam. Engineered: yes

Source:

Homo sapiens. Human. Organism_taxid: 9606. Expressed in: spodoptera frugiperda. Expression_system_taxid: 7108. Expression_system_cell_line: sf9.

Resolution:

2.74Å R-factor: 0.183 R-free: 0.237

Authors:

S.Munnich,M.H.Taft,S.Pathan-Chhatbar,D.J.Manstein

Key ref:

S.Münnich et al. (2014). Crystal structure of human myosin 1c--the motor in GLUT4 exocytosis: implications for Ca2+ regulation and 14-3-3 binding. J Mol Biol, 426, 2070-2081. PubMed id: 24636949 DOI: 10.1016/j.jmb.2014.03.004

Date:

19-Jul-13 Release date: 26-Mar-14

Protein chains

O00159  (MYO1C_HUMAN) -  Unconventional myosin-Ic from Homo sapiens

Seq: 1063 a.a.

Struc: 698 a.a.

Protein chains

P0DP23  (CALM1_HUMAN) -  Calmodulin-1 from Homo sapiens

Seq: 149 a.a.

Struc: 148 a.a.

Enzyme reactions

• Enzyme class: Chains A, C: E.C.3.6.4.1 - Transferred entry: 5.6.1.8.
• Reaction: ATP + H₂O = ADP + phosphate

ATP + H(2)O = ADP (Bound ligand (Het Group name = AOV) matches with 84.38% similarity) + phosphate

Molecule diagrams generated from .mol files obtained from the KEGG ftp site

reference

DOI no: 10.1016/j.jmb.2014.03.004

J Mol Biol 426:2070-2081 (2014)

PubMed id: 24636949

Crystal structure of human myosin 1c--the motor in GLUT4 exocytosis: implications for Ca2+ regulation and 14-3-3 binding.

S.Münnich, M.H.Taft, D.J.Manstein.

ABSTRACT

Myosin 1c (Myo1c) plays a key role in supporting motile events that underlie cell migration, vesicle trafficking, insulin-stimulated glucose uptake and hearing. Here, we present the crystal structure of the human Myo1c motor in complex with its light chain calmodulin. Our structure reveals tight interactions of the motor domain with calmodulin bound to the first IQ motif in the neck region. Several of the calmodulin residues contributing to this interaction are also involved in Ca(2+) binding. Contact residues in the motor domain are linked to the central β-sheet and the HO helix, suggesting a mechanism for communicating changes in Ca(2+) binding in the neck region to the actin and nucleotide binding regions of the motor domain. The structural context and the chemical environment of Myo1c mutations that are involved in sensorineural hearing loss in humans are described and their impact on motor function is discussed. We show that a construct consisting of the motor domain of Myo1c and the first IQ motif is sufficient to establish a tight interaction with 14-3-3β (KD=0.9μM) and present the model of a double-headed Myo1c-14-3-3 complex. This complex has been implicated in the exocytosis of glucose transporter 4 storage vesicles during insulin-stimulated glucose uptake.