The mesa trail and the interacting heads motif of myosin II.
IHM
Interacting heads motif
Mesa trail
Myosin II mesa
Myosin head
Subfragment 2
Journal
Archives of biochemistry and biophysics
ISSN: 1096-0384
Titre abrégé: Arch Biochem Biophys
Pays: United States
ID NLM: 0372430
Informations de publication
Date de publication:
15 02 2020
15 02 2020
Historique:
received:
03
10
2019
revised:
09
12
2019
accepted:
12
12
2019
pubmed:
18
12
2019
medline:
12
5
2020
entrez:
18
12
2019
Statut:
ppublish
Résumé
Myosin II molecules in the thick filaments of striated muscle form a structure in which the heads interact with each other and fold back onto the tail. This structure, the "interacting heads motif" (IHM), provides a mechanistic basis for the auto-inhibition of myosin in relaxed thick filaments. Similar IHM interactions occur in single myosin molecules of smooth and nonmuscle cells in the switched-off state. In addition to the interaction between the two heads, which inhibits their activity, the IHM also contains an interaction between the motor domain of one head and the initial part (subfragment 2, S2) of the tail. This is thought to be a crucial anchoring interaction that holds the IHM in place on the thick filament. S2 appears to cross the head at a specific location within a broader region of the motor domain known as the myosin mesa. Here, we show that the positive and negative charge distribution in this part of the mesa is complementary to the charge distribution on S2. We have designated this the "mesa trail" owing to its linear path across the mesa. We studied the structural sequence alignment, the location of charged residues on the surface of myosin head atomic models, and the distribution of surface charge potential along the mesa trail in different types of myosin II and in different species. The charge distribution in both the mesa trail and the adjacent S2 is relatively conserved. This suggests a common basis for IHM formation across different myosin IIs, dependent on attraction between complementary charged patches on S2 and the myosin head. Conservation from mammals to insects suggests that the mesa trail/S2 interaction plays a key role in the inhibitory function of the IHM.
Identifiants
pubmed: 31843643
pii: S0003-9861(19)30877-X
doi: 10.1016/j.abb.2019.108228
pmc: PMC6939892
mid: NIHMS1547236
pii:
doi:
Substances chimiques
Arthropod Proteins
0
Protozoan Proteins
0
Myosin Type II
EC 3.6.1.-
Types de publication
Journal Article
Research Support, N.I.H., Extramural
Langues
eng
Sous-ensembles de citation
IM
Pagination
108228Subventions
Organisme : NIAMS NIH HHS
ID : R01 AR067279
Pays : United States
Organisme : NIAMS NIH HHS
ID : R01 AR072036
Pays : United States
Organisme : NHLBI NIH HHS
ID : R01 HL139883
Pays : United States
Informations de copyright
Copyright © 2019 Elsevier Inc. All rights reserved.
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